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1GSN

HUMAN GLUTATHIONE REDUCTASE MODIFIED BY DINITROSOGLUTATHIONE

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 Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 1031
ChainResidue
AARG218
AHIS219
AARG224
AHOH519
AHOH590
AHOH615
AHOH851

site_idAC2
Number of Residues36
DetailsBINDING SITE FOR RESIDUE FAD A 499
ChainResidue
ASER30
AGLY31
AGLU50
ASER51
AHIS52
AGLY56
ATHR57
ACYS58
ACSO63
ALYS66
AGLY128
AHIS129
AALA130
AALA155
ATHR156
AGLY157
ATYR197
AARG291
AGLY330
AASP331
ALEU337
ALEU338
ATHR339
APRO340
AHIS467
APRO468
AHOH502
AHOH504
AHOH510
AHOH515
AHOH554
AHOH826
AHOH859
AHOH864
AGLY27
AGLY29

site_idAC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE GSH A 1030
ChainResidue
ASER30
AALA34
AARG37
ACYS58
AVAL59
ATYR114
ATHR339
AILE343
AARG347
AHIS467
ATHR476
AHOH516
AHOH558
AHOH560
AHOH810
AHOH812
AHOH1026

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
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AHIS467

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING:
ChainResidueDetails
AGLU50

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P47791
ChainResidueDetails
ALYS53

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

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1get
ChainResidueDetails
ACYS58
AGLU201
ATYR197
ALYS66

site_idMCSA1
Number of Residues7
DetailsM-CSA 6
ChainResidueDetails
ACYS58electrofuge, electrophile, nucleofuge, nucleophile
ACSO63electrofuge, electrophile, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
ALYS66activator, electrostatic stabiliser, hydrogen bond donor
ATYR197activator
AGLU201activator, electrostatic stabiliser, hydrogen bond acceptor
AHIS467hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AGLU472activator, electrostatic stabiliser, hydrogen bond acceptor

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PDB entries from 2024-11-13

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