Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1GRG

SUBSTRATE BINDING AND CATALYSIS BY GLUTATHIONE REDUCTASE AS DERIVED FROM REFINED ENZYME: SUBSTRATE CRYSTAL STRUCTURES AT 2 ANGSTROMS RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0004362molecular_functionglutathione-disulfide reductase (NADPH) activity
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0005829cellular_componentcytosol
A0006749biological_processglutathione metabolic process
A0009055molecular_functionelectron transfer activity
A0009897cellular_componentexternal side of plasma membrane
A0016491molecular_functionoxidoreductase activity
A0016668molecular_functionoxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
A0034599biological_processcellular response to oxidative stress
A0045454biological_processcell redox homeostasis
A0050660molecular_functionflavin adenine dinucleotide binding
A0050661molecular_functionNADP binding
A0070062cellular_componentextracellular exosome
A0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 480
ChainResidue
AHIS219
AARG224
AHOH505
AHOH575
AHOH600

site_idAC2
Number of Residues38
DetailsBINDING SITE FOR RESIDUE FAD A 479
ChainResidue
AGLU50
ASER51
AHIS52
AGLY56
ATHR57
A0A858
AVAL61
AGLY62
ACYS63
ALYS66
AGLY128
AHIS129
AALA130
AALA155
ATHR156
AGLY157
ATYR197
AARG291
AGLY330
AASP331
ALEU337
ALEU338
ATHR339
APRO340
AHIS467
APRO468
AHOH488
AHOH490
AHOH496
AHOH501
AHOH540
AHOH810
AHOH847
AHOH1006
AGLY27
AGLY29
ASER30
AGLY31

Functional Information from PROSITE/UniProt
site_idPS00076
Number of Residues11
DetailsPYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGtCVnvGCVP
ChainResidueDetails
AGLY55-PRO65

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING:
ChainResidueDetails
APHE94

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P47791
ChainResidueDetails
AARG97

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
AHIS467
AGLU472

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
A0A858
AGLU201
ATYR197
ALYS66
ACYS63

site_idMCSA1
Number of Residues5
DetailsM-CSA 6
ChainResidueDetails
ALYS102electrofuge, electrophile, nucleofuge, nucleophile
AVAL107electrofuge, electrophile, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
ALEU110activator, electrostatic stabiliser, hydrogen bond donor
AALA241activator
AVAL245activator, electrostatic stabiliser, hydrogen bond acceptor

219140

PDB entries from 2024-05-01

PDB statisticsPDBj update infoContact PDBjnumon