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2GRT

HUMAN GLUTATHIONE REDUCTASE A34E, R37W MUTANT, OXIDIZED GLUTATHIONE COMPLEX

Functional Information from GO Data
ChainGOidnamespacecontents
A0004362molecular_functionglutathione-disulfide reductase (NADPH) activity
A0006749biological_processglutathione metabolic process
A0016491molecular_functionoxidoreductase activity
A0016668molecular_functionoxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
A0045454biological_processcell redox homeostasis
A0050660molecular_functionflavin adenine dinucleotide binding
A0050661molecular_functionNADP binding
Functional Information from PDB Data
site_idAC1
Number of Residues33
DetailsBINDING SITE FOR RESIDUE FAD A 479
ChainResidue
ALYS53
AGLY56
ATHR57
ACYS58
AVAL61
AGLY62
ACYS63
ALYS66
AGLY128
AHIS129
AILE26
AALA130
AALA155
ATHR156
AGLY157
ATYR197
AARG291
AGLY330
AASP331
ALEU337
ALEU338
AGLY27
ATHR339
APRO340
AALA342
AHIS467
APRO468
AGLY29
ASER30
AGLY31
AGLU50
ASER51
AHIS52

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE GDS A 481
ChainResidue
ASER30
AGLU34
ATRP37
AVAL59
AVAL64
ATYR106
ALEU110
AILE113
ATYR114
AASN117
AILE343
APHE403
AMET406
AHIS467
ATHR469
AGLU472
AGLU473
ATHR476

site_idS1
Number of Residues1
DetailsTHE ACTIVE SITE HISTIDINE (HIS 467) IS FROM THE OTHER SUBUNIT.
ChainResidue
AHIS467

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
ACYS58
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

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PDB entries from 2024-05-01

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