University of California San Francisco | About UCSF | UCSF Benioff Children's Hospital San Francisco

ModBase: Database of Comparative Protein Structure Models

Model Details Page

Sequence Information

Primary Database Link P06715.1
Original Database ID ref NP_417957.1
Organism Escherichia coli, Escherichia coli K-12, etc.
Annotation gshr_ecoli recname: full=glutathione
reductase; short=gr; short=grase
Sequence Length 450

Dataset Information:

The newest dataset for this sequence was created on 2016-11-09. If you think that a better template has been added to the template database since, you can start a new calculation.

The calculation typically takes 1-2 days, and the results will be added to this page. Registered users will receive an email notification.

Information for additional models of this sequences are available by clicking on the model thumbnails below.  

Model Information

Perform action on this model:

Quality criteria indicate whether the model is considered
reliable (green)
or unreliable (red).
 
Target Region3-450
Protein Length450
Template PDB Code1gesA
Template Region3-450
Sequence Identity98%
E-Value0
GA3411
MPQS2.17776
z-DOPE-1.11
TSVMod MethodMTALL
TSVMod RMSD0.953
TSVMod NO350.962
DatasetMW-e_coli_D1
ModPipe VersionSVN.r1602
Model Date2016-11-09

Mouse over the images for more information

Sequence Model Coverage Summary
for all Models of this Sequence:

Filtered models for current sequence (Show all models)

 

Cross-references

Show obsolete/secondary identifiers
Template Structure
PDB1gesanatomy of an engineered nad-binding site ; EC: 1.8.1.7 ; PFAM: PF00070 PF02852 ; SCOP: 30473 30474 40168
DBALI1gesA 
CATH3.50.50.60 Domain: 1gesA01 FAD/NAD(P)-binding domain (100%)
CATH3.50.50.60 Domain: 1gesA02 FAD/NAD(P)-binding domain (100%)
CATH3.30.390.30 Domain: 1gesA03 Enolase-like; domain 1 (100%)
JenaImageLibrary1ges 
Target Sequence
UniProtKBA0A094VUJ5SubName: Full=Glutathione reductase {ECO:0000313|EMBL:AKO54669.1};EC=1.8.1.7 {ECO:0000313|EMBL:AKO54669.1};SubName: Full=Glutathione-disulfide reductase;EC=1.8.1.7;
InterProA0A094VUJ5 
PFAMA0A094VUJ5 
ProdomA0A094VUJ5 
UniProtKBF9R5H5SubName: Full=Glutathione reductase;EC=1.8.1.7;
InterProF9R5H5 
PFAMF9R5H5 
ProdomF9R5H5 
UniProtKBH0Q7M9SubName: Full=Glutathione oxidoreductase;
InterProH0Q7M9 
PFAMH0Q7M9 
ProdomH0Q7M9 
UniProtKBI0ZXU3SubName: Full=Glutathione oxidoreductase;
InterProI0ZXU3 
PFAMI0ZXU3 
ProdomI0ZXU3 
UniProtKBC9QVP8SubName: Full=Glutathione reductase;SubName: Full=Glutathione-disulfide reductase;
InterProC9QVP8 
PFAMC9QVP8 
ProdomC9QVP8 
UniProtKBP06715RecName: Full=Glutathione reductase;Short=GR;Short=GRase;EC=1.8.1.7;
InterProP06715 
PFAMP06715 
ProdomP06715 
UniProtKBB1X7V5SubName: Full=Glutathione oxidoreductase;
InterProB1X7V5 
PFAMB1X7V5 
ProdomB1X7V5 
UniProtKBG2F9V7SubName: Full=Glutathione reductase;EC=1.8.1.7;
InterProG2F9V7 
PFAMG2F9V7 
ProdomG2F9V7 
UniProtKBA0A0G3I2P0SubName: Full=Glutathione oxidoreductase protein {ECO:0000313|EMBL:AKK19215.1};
InterProA0A0G3I2P0 
PFAMA0A0G3I2P0 
ProdomA0A0G3I2P0 
UniProtKBQ2M7G2RecName: Full=Glutathione reductase;Short=GR;Short=GRase;EC=1.8.1.7;
InterProQ2M7G2 
PFAMQ2M7G2 
ProdomQ2M7G2 
UniProtKBC4ZW47SubName: Full=Glutathione oxidoreductase;
InterProC4ZW47 
PFAMC4ZW47 
ProdomC4ZW47 
UniProtKBA0A2S5ZPY5SubName: Full=Glutathione reductase {ECO:0000313|EMBL:SVF18000.1}SubName: Full=Glutathione-disulfide reductase {ECO:0000313|EMBL:QGF36415.1}EC=1.8.1.7 {ECO:0000313|EMBL:QGF36415.1, ECO:0000313|EMBL:SV
InterProA0A2S5ZPY5 
PFAMA0A2S5ZPY5 
ProdomA0A2S5ZPY5 
UniProtKBF9R5H5SubName: Full=Glutathione reductase;EC=1.8.1.7;
InterProF9R5H5 
PFAMF9R5H5 
ProdomF9R5H5 
UniProtKBA0A5Q3TFN3SubName: Full=Glutathione-disulfide reductase {ECO:0000313|EMBL:QGL42700.1}EC=1.8.1.7 {ECO:0000313|EMBL:QGL42700.1}
InterProA0A5Q3TFN3 
PFAMA0A5Q3TFN3 
ProdomA0A5Q3TFN3 
UniProtKBC9QVP8SubName: Full=Glutathione reductase;SubName: Full=Glutathione-disulfide reductase;
InterProC9QVP8 
PFAMC9QVP8 
ProdomC9QVP8 
UniProtKBG2F9V7SubName: Full=Glutathione reductase;EC=1.8.1.7;
InterProG2F9V7 
PFAMG2F9V7 
ProdomG2F9V7 
UniProtKBC4ZW47SubName: Full=Glutathione oxidoreductase;
InterProC4ZW47 
PFAMC4ZW47 
ProdomC4ZW47 
UniProtKBA0A8F2PPW6SubName: Full=Glutathione-disulfide reductase {ECO:0000313|EMBL:QWV47785.1}EC=1.8.1.7 {ECO:0000313|EMBL:QWV47785.1}
InterProA0A8F2PPW6 
PFAMA0A8F2PPW6 
ProdomA0A8F2PPW6 
UniProtKBB1X7V5SubName: Full=Glutathione oxidoreductase;
InterProB1X7V5 
PFAMB1X7V5 
ProdomB1X7V5 
UniProtKBA0A8F9HBL9SubName: Full=Glutathione-disulfide reductase {ECO:0000313|EMBL:QYE25944.1}EC=1.8.1.7 {ECO:0000313|EMBL:QYE25944.1}
InterProA0A8F9HBL9 
PFAMA0A8F9HBL9 
ProdomA0A8F9HBL9 
UniProtKBA0A8F8GYW0SubName: Full=Glutathione-disulfide reductase {ECO:0000313|EMBL:QXZ37166.1}EC=1.8.1.7 {ECO:0000313|EMBL:QXZ37166.1}
InterProA0A8F8GYW0 
PFAMA0A8F8GYW0 
ProdomA0A8F8GYW0 
UniProtKBQ2M7G2Glutathione oxidoreductase
InterProQ2M7G2 
PFAMQ2M7G2 
ProdomQ2M7G2 
UniProtKBH0Q7M9SubName: Full=Glutathione oxidoreductase;
InterProH0Q7M9 
PFAMH0Q7M9 
ProdomH0Q7M9 
UniProtKBI0ZXU3SubName: Full=Glutathione oxidoreductase;
InterProI0ZXU3 
PFAMI0ZXU3 
ProdomI0ZXU3 
UniProtKBP06715RecName: Full=Glutathione reductase;Short=GR;Short=GRase;EC=1.8.1.7;
InterProP06715 
PFAMP06715 
ProdomP06715 
UniProtKBP06715.1GSHR_ECOLI RecName: Full=Glutathione reductase; Short=GR; Short=GRase
InterProP06715.1 
PFAMP06715.1 
ProdomP06715.1 
UniProtKBQ2M7G2RecName: Full=Glutathione reductase;Short=GR;Short=GRase;EC=1.8.1.7;
InterProQ2M7G2 
PFAMQ2M7G2 
ProdomQ2M7G2 
RefSeqNP_417957.1 glutathione oxidoreductase [Escherichia coli str. K-12 substr. MG1655]
RefSeqYP_002928385.1 glutathione oxidoreductase [Escherichia coli BW2952]
RefSeqYP_001732331.1 glutathione oxidoreductase [Escherichia coli str. K-12 substr. DH10B]
RefSeqAP_004293.1 glutathione oxidoreductase [Escherichia coli str. K-12 substr. W3110]
PDB1GERAChain A, The Structure Of Glutathione Reductase From Escherichia Coli At 1.86 Angstroms Resolution: Comparison With The Enzyme From Human Erythrocytes
PDB1GERB Chain B, The Structure Of Glutathione Reductase From Escherichia Coli At 1.86 Angstroms Resolution: Comparison With The Enzyme From Human Erythrocytes
PDB1GETB Chain B, Anatomy Of An Engineered Nad-Binding Site
PDB1GETAChain A, Anatomy Of An Engineered Nad-Binding Site
PDB1GETBChain B, Anatomy Of An Engineered Nad-Binding Site
PDB1GERBChain B, The Structure Of Glutathione Reductase From Escherichia Coli At 1.86 Angstroms Resolution: Comparison With The Enzyme From Human Erythrocytes
GenPept899733213glutathione reductase
GenPept932861594Glutathione reductase
GenPept809423B Chain B, Anatomy Of An Engineered Nad-Binding Site
GenPept121674GSHR_ECOLI RecName: Full=Glutathione reductase; Short=GR; Short=GRase
GenPept899728730glutathione reductase
GenPept899724375glutathione reductase
GenPept47266180Sequence 398 from patent US 6720139
GenPept549814835glutathione oxidoreductase
GenPept557273306glutathione reductase
GenPept66121RDECU glutathione reductase (NADPH) (EC 1.6.4.2) - Escherichia coli
GenPept664685829glutathione reductase
GenPept682120900glutathione oxidoreductase
GenPept687674555glutathione reductase (NADPH)
GenPept687678592glutathione reductase (NADPH)
GenPept466637glutathione oxidoreductase
GenPept359333654glutathione oxidoreductase
GenPept16131372 glutathione oxidoreductase [Escherichia coli str. K-12 substr. MG1655]
GenPept169890846glutathione oxidoreductase
GenPept170083011 glutathione oxidoreductase [Escherichia coli str. K-12 substr. DH10B]
GenPept1789915glutathione oxidoreductase
GenPept238861350glutathione oxidoreductase
GenPept238902589 glutathione oxidoreductase [Escherichia coli BW2952]
GenPept260447486glutathione-disulfide reductase
GenPept315138074glutathione reductase
GenPept732682696glutathione reductase
GenPept808736759glutathione reductase
GenPept817580813glutathione oxidoreductase
GenPept817584952glutathione oxidoreductase
GenPept817589093glutathione oxidoreductase
GenPept817593233glutathione oxidoreductase
GenPept827618745glutathione oxidoreductase protein
GenPept827623481glutathione oxidoreductase protein
GenPept85676544glutathione oxidoreductase
GenPept89110513 glutathione oxidoreductase [Escherichia coli str. K-12 substr. W3110]
GenPept817576671glutathione oxidoreductase
GenPept146248glutathione reductase (EC 1.6.4.2)
GenPept809418A Chain A, The Structure Of Glutathione Reductase From Escherichia Coli At 1.86 Angstroms Resolution: Comparison With The Enzyme From Human Erythrocytes
GenPept809419B Chain B, The Structure Of Glutathione Reductase From Escherichia Coli At 1.86 Angstroms Resolution: Comparison With The Enzyme From Human Erythrocytes
GenPept809422A Chain A, Anatomy Of An Engineered Nad-Binding Site
GenBankACX37908.1 glutathione-disulfide reductase [Escherichia coli DH1]
GenBankACR63348.1 glutathione oxidoreductase [Escherichia coli BW2952]
GenBankACB04553.1 glutathione oxidoreductase [Escherichia coli str. K-12 substr. DH10B]
GenBankAAC76525.1 glutathione oxidoreductase [Escherichia coli str. K-12 substr. MG1655]
GenBankAAB18476.1 glutathione oxidoreductase [Escherichia coli str. K-12 substr. MG1655]
GenBankAAA23926.1 glutathione reductase (EC 1.6.4.2) [Escherichia coli]