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Sequence Information

Primary Database Link P08200.1
Original Database ID sp P08200.1
Organism Escherichia coli, Escherichia coli K-12, etc.
Annotation idh_ecoli recname: full=isocitrate
dehydrogenase [nadp]; short=idh;
altname: ful l=idp; altname: full=nadp(+)-specific
icdh; altname: full=oxalosuccin
...
Sequence Length 416

Dataset Information:

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Model Information

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Target Region1-416
Protein Length416
Template PDB Code1pb1A
Template Region1-416
Sequence Identity100%
E-Value0
GA3411
MPQS2.2047
z-DOPE-1.1
TSVMod MethodMTALL
TSVMod RMSD2.38
TSVMod NO350.952
DatasetMW-e_coli_D1
ModPipe VersionSVN.r1602
Model Date2016-11-09

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Cross-references

Show obsolete/secondary identifiers
Template Structure
PDB1pb1a four location model to explain the stereospecificity of proteins. ; EC: 1.1.1.42 ; PFAM: PF00180
DBALI1pb1A 
CATH3.40.718.10 Domain: 1pb1A00 Isopropylmalate Dehydrogenase (100%)
JenaImageLibrary1pb1 
Target Sequence
UniProtKBC9QYH6RecName: Full=Isocitrate dehydrogenase [NADP];EC=1.1.1.42;
InterProC9QYH6 
PFAMC9QYH6 
ProdomC9QYH6 
UniProtKBG2F4F9RecName: Full=Isocitrate dehydrogenase [NADP];EC=1.1.1.42;
InterProG2F4F9 
PFAMG2F4F9 
ProdomG2F4F9 
UniProtKBH0Q9W1RecName: Full=Isocitrate dehydrogenase [NADP];EC=1.1.1.42;
InterProH0Q9W1 
PFAMH0Q9W1 
ProdomH0Q9W1 
UniProtKBI0ZQV3RecName: Full=Isocitrate dehydrogenase [NADP];EC=1.1.1.42;
InterProI0ZQV3 
PFAMI0ZQV3 
ProdomI0ZQV3 
UniProtKBM2NYT7RecName: Full=Isocitrate dehydrogenase [NADP];EC=1.1.1.42;
InterProM2NYT7 
PFAMM2NYT7 
ProdomM2NYT7 
UniProtKBA0A094WK83RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|RuleBase:RU004446};EC=1.1.1.42 {ECO:0000256|RuleBase:RU004446};
InterProA0A094WK83 
PFAMA0A094WK83 
ProdomA0A094WK83 
UniProtKBP08200RecName: Full=Isocitrate dehydrogenase [NADP];Short=IDH;EC=1.1.1.42;AltName: Full=IDP;AltName: Full=NADP(+)-specific ICDH;AltName: Full=Oxalosuccinate decarboxylase;
InterProP08200 
PFAMP08200 
ProdomP08200 
UniProtKBA0A3U1JXT1Isocitrate dehydrogenase [NADP] {ECO:0000256|RuleBase:RU004446}EC=1.1.1.42 {ECO:0000256|RuleBase:RU004446}
InterProA0A3U1JXT1 
PFAMA0A3U1JXT1 
ProdomA0A3U1JXT1 
UniProtKBC9QYH6RecName: Full=Isocitrate dehydrogenase [NADP];EC=1.1.1.42;
InterProC9QYH6 
PFAMC9QYH6 
ProdomC9QYH6 
UniProtKBA0A8F8DCK5SubName: Full=NADP-dependent isocitrate dehydrogenase {ECO:0000313|EMBL:QXZ35342.1}
InterProA0A8F8DCK5 
PFAMA0A8F8DCK5 
ProdomA0A8F8DCK5 
UniProtKBA0A5Q3TIW9Isocitrate dehydrogenase [NADP] {ECO:0000256|RuleBase:RU004446}EC=1.1.1.42 {ECO:0000256|RuleBase:RU004446}
InterProA0A5Q3TIW9 
PFAMA0A5Q3TIW9 
ProdomA0A5Q3TIW9 
UniProtKBI0ZQV3RecName: Full=Isocitrate dehydrogenase [NADP];EC=1.1.1.42;
InterProI0ZQV3 
PFAMI0ZQV3 
ProdomI0ZQV3 
UniProtKBA0A8F9H893SubName: Full=NADP-dependent isocitrate dehydrogenase {ECO:0000313|EMBL:QYE24183.1}
InterProA0A8F9H893 
PFAMA0A8F9H893 
ProdomA0A8F9H893 
UniProtKBG2F4F9RecName: Full=Isocitrate dehydrogenase [NADP];EC=1.1.1.42;
InterProG2F4F9 
PFAMG2F4F9 
ProdomG2F4F9 
UniProtKBH0Q9W1RecName: Full=Isocitrate dehydrogenase [NADP];EC=1.1.1.42;
InterProH0Q9W1 
PFAMH0Q9W1 
ProdomH0Q9W1 
UniProtKBP08200RecName: Full=Isocitrate dehydrogenase [NADP];Short=IDH;EC=1.1.1.42;AltName: Full=IDP;AltName: Full=NADP(+)-specific ICDH;AltName: Full=Oxalosuccinate decarboxylase;
InterProP08200 
PFAMP08200 
ProdomP08200 
UniProtKBP08200.1IDH_ECOLI RecName: Full=Isocitrate dehydrogenase [NADP]; Short=IDH; AltName: Full=IDP; AltName: Full=NADP(+)-specific ICDH; AltName: Full=Oxalosuccinate decarboxylase
InterProP08200.1 
PFAMP08200.1 
ProdomP08200.1 
RefSeqAP_001762.1 isocitrate dehydrogenase, specific for NADP+ [Escherichia coli str. K-12 substr. W3110]
RefSeqNP_415654.1 e14 prophage; isocitrate dehydrogenase, specific for NADP+ [Escherichia coli str. K-12 substr. MG1655]
PDB5ICDAChain A, Regulation Of An Enzyme By Phosphorylation At The Active Site
PDB9ICDAChain A, Catalytic Mechanism Of Nadp+-Dependent Isocitrate Dehydrogenase: Implications From The Structures Of Magnesium-Isocitrate And Nadp+ Complexes
PDB9ICDA Chain A, Catalytic Mechanism Of Nadp+-Dependent Isocitrate Dehydrogenase: Implications From The Structures Of Magnesium-Isocitrate And Nadp+ Complexes
PDB1PB1A Chain A, A Four Location Model To Explain The Stereospecificity Of Proteins.
PDB3ICDA Chain A, Structure Of A Bacterial Enzyme Regulated By Phosphorylation, Isocitrate Dehydrogenase
PDB3ICDAChain A, Structure Of A Bacterial Enzyme Regulated By Phosphorylation, Isocitrate Dehydrogenase
PDB3LCBD Chain D, The Crystal Structure Of Isocitrate Dehydrogenase KinasePHOSPHATASE In Complex With Its Substrate, Isocitrate Dehydrogenase, From Escherichia Coli.
PDB3LCBCChain C, The Crystal Structure Of Isocitrate Dehydrogenase KinasePHOSPHATASE In Complex With Its Substrate, Isocitrate Dehydrogenase, From Escherichia Coli.
PDB3LCBDChain D, The Crystal Structure Of Isocitrate Dehydrogenase KinasePHOSPHATASE In Complex With Its Substrate, Isocitrate Dehydrogenase, From Escherichia Coli.
PDB4AJ3AChain A, 3d Structure Of E. Coli Isocitrate Dehydrogenase In Complex With Isocitrate, Calcium(ii) And Nadp - The Pseudo-michaelis Complex
PDB5ICDA Chain A, Regulation Of An Enzyme By Phosphorylation At The Active Site
PDB4AJAAChain A, 3d Structure Of E. Coli Isocitrate Dehydrogenase In Complex With Isocitrate, Calcium(Ii) And Thionadp
PDB1PB3A Chain A, Sites Of Binding And Orientation In A Four Location Model For Protein Stereospecificity.
PDB1AI2A Chain A, Isocitrate Dehydrogenase Complexed With Isocitrate, Nadp+, And Calcium (Flash-Cooled)
PDB1AI2AChain A, Isocitrate Dehydrogenase Complexed With Isocitrate, Nadp+, And Calcium (flash-cooled)
PDB1AI3A Chain A, Orbital Steering In The Catalytic Power Of Enzymes: Small Structural Changes With Large Catalytic Consequences
PDB1AI3AChain A, Orbital Steering In The Catalytic Power Of Enzymes: Small Structural Changes With Large Catalytic Consequences
PDB1IKAA Chain A, Structure Of Isocitrate Dehydrogenase With Alpha- Ketoglutarate At 2.7 Angstroms Resolution: Conformational Changes Induced By Decarboxylation Of Isocitrate
PDB1IKAAChain A, Structure Of Isocitrate Dehydrogenase With Alpha-Ketoglutarate At 2.7 Angstroms Resolution: Conformational Changes Induced By Decarboxylation Of Isocitrate
PDB1P8FA Chain A, A Four Location Model To Explain The Stereospecificity Of Proteins.
PDB1P8FAChain A, A Four Location Model To Explain The Stereospecificity Of Proteins.
PDB1PB3AChain A, Sites Of Binding And Orientation In A Four Location Model For Protein Stereospecificity.
PDB1SJSA Chain A, Access To Phosphorylation In Isocitrate Dehydrogenase May Occur By Domain Shifting
PDB1PB1AChain A, A Four Location Model To Explain The Stereospecificity Of Proteins.
PDB1SJSAChain A, Access To Phosphorylation In Isocitrate Dehydrogenase May Occur By Domain Shifting
GenPept817578589isocitrate dehydrogenase, e14 prophage attachment site, tellurite reductase
GenPept817574447isocitrate dehydrogenase, e14 prophage attachment site, tellurite reductase
GenPept915303590Sequence 54726 from patent US 8952217
GenPept808708637isocitrate dehydrogenase
GenPept808704263isocitrate dehydrogenase
GenPept899722120isocitrate dehydrogenase
GenPept817582728isocitrate dehydrogenase, e14 prophage attachment site, tellurite reductase
GenPept817586869isocitrate dehydrogenase, e14 prophage attachment site, tellurite reductase
GenPept167273996Sequence 798 from patent US 7314974
GenPept915275968Sequence 27884 from patent US 8952217
GenPept899730870isocitrate dehydrogenase
GenPept899726475isocitrate dehydrogenase
GenPept817591010isocitrate dehydrogenase, e14 prophage attachment site, tellurite reductase
GenPept89107982 isocitrate dehydrogenase, specific for NADP+ [Escherichia coli str. K-12 substr. W3110]
GenPept808699888isocitrate dehydrogenase
GenPept757003413Sequence 429 from patent US 8883464
GenPept732684942isocitrate dehydrogenase
GenPept2313289ICD Chain , Isocitrate Dehydrogenase (E.C.1.1.1.42) Complex With NADP+
GenPept2311535ICD Chain , Isocitrate Dehydrogenase (E.C.1.1.1.42) Complex With Mg2+ And Isocitrate
GenPept2308853ICD Chain , Isocitrate Dehydrogenase (E.C.1.1.1.42)
GenPept124171IDH_ECOLI RecName: Full=Isocitrate dehydrogenase [NADP]; Short=IDH; AltName: Full=IDP; AltName: Full=NADP(+)-specific ICDH; AltName: Full=Oxalosuccinate decarboxylase
GenPept1787381isocitrate dehydrogenase; e14 prophage attachment site; tellurite reductase
GenPept1651566Isocitrate dehydrogenase (NADP
GenPept1651560isocitrate dehydrogenase, specific for NADP+
GenPept16129099 e14 prophage; isocitrate dehydrogenase, specific for NADP+ [Escherichia coli str. K-12 substr. MG1655]
GenPept157837189A Chain A, Catalytic Mechanism Of Nadp+-Dependent Isocitrate Dehydrogenase: Implications From The Structures Of Magnesium-Isocitrate And Nadp+ Complexes
GenPept157837047A Chain A, Regulation Of An Enzyme By Phosphorylation At The Active Site
GenPept157836827A Chain A, Structure Of A Bacterial Enzyme Regulated By Phosphorylation, Isocitrate Dehydrogenase
GenPept157833817A Chain A, Access To Phosphorylation In Isocitrate Dehydrogenase May Occur By Domain Shifting
GenPept157831458A Chain A, Structure Of Isocitrate Dehydrogenase With Alpha-Ketoglutarate At 2.7 Angstroms Resolution: Conformational Changes Induced By Decarboxylation Of Isocitrate
GenPept157829890A Chain A, Orbital Steering In The Catalytic Power Of Enzymes: Small Structural Changes With Large Catalytic Consequences
GenPept157829889A Chain A, Isocitrate Dehydrogenase Complexed With Isocitrate, Nadp+, And Calcium (flash-cooled)
GenPept260449725isocitrate dehydrogenase, NADP-dependent
GenPept26245551AI3 Chain , Orbital Steering In The Catalytic Power Of Enzymes: Small Structural Changes With Large Catalytic Consequences
GenPept26248691AI2 Chain , Isocitrate Dehydrogenase Complexed With Isocitrate, Nadp+, And Calcium (Flash-Cooled)
GenPept359331789e14 prophage; isocitrate dehydrogenase, specific for NADP+
GenPept383249102Sequence 4 from patent US 8143036
GenPept410562660A Chain A, 3d Structure Of E. Coli Isocitrate Dehydrogenase In Complex With Isocitrate, Calcium(ii) And Nadp - The Pseudo-michaelis Complex
GenPept410562661A Chain A, 3d Structure Of E. Coli Isocitrate Dehydrogenase In Complex With Isocitrate, Calcium(Ii) And Thionadp
GenPept549812639e14 prophage; isocitrate dehydrogenase, specific for NADP+
GenPept5761811IKA Chain , Isocitrate Dehydrogenase (E.C.1.1.1.42) Complexed With Alpha-Ketoglutarate
GenPept65942DCECIS isocitrate dehydrogenase (NADP+) (EC 1.1.1.42) [validated] - Escherichia coli
GenPept682118673e14 prophage; isocitrate dehydrogenase, specific for NADP+
GenPept33358035A Chain A, Sites Of Binding And Orientation In A Four Location Model For Protein Stereospecificity.
GenPept33358034A Chain A, A Four Location Model To Explain The Stereospecificity Of Proteins.
GenPept27811051SJS Chain , Access To Phosphorylation In Isocitrate Dehydrogenase May Occur By Domain Shifting
GenPept294979773C Chain C, The Crystal Structure Of Isocitrate Dehydrogenase KinasePHOSPHATASE In Complex With Its Substrate, Isocitrate Dehydrogenase, From Escherichia Coli.
GenPept146432isocitrate dehydrogenase (icd; EC 1.1.1.42)
GenPept294979774D Chain D, The Crystal Structure Of Isocitrate Dehydrogenase KinasePHOSPHATASE In Complex With Its Substrate, Isocitrate Dehydrogenase, From Escherichia Coli.
GenPept315135768e14 prophage; isocitrate dehydrogenase, specific for NADP+
GenPept31616007A Chain A, A Four Location Model To Explain The Stereospecificity Of Proteins.
GenBankACX40147.1 isocitrate dehydrogenase, NADP-dependent [Escherichia coli DH1]
GenBankAAA24006.1 isocitrate dehydrogenase (icd; EC 1.1.1.42) [Escherichia coli]
GenBankAAC74220.1 e14 prophage; isocitrate dehydrogenase, specific for NADP+ [Escherichia coli str. K-12 substr. MG1655]