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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1BWC

STRUCTURE OF HUMAN GLUTATHIONE REDUCTASE COMPLEXED with AJOENE INHIBITOR AND SUBVERSIVE SUBSTRATE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004362	molecular_function	glutathione-disulfide reductase (NADPH) activity
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0005829	cellular_component	cytosol
A	0006749	biological_process	glutathione metabolic process
A	0009055	molecular_function	electron transfer activity
A	0009897	cellular_component	external side of plasma membrane
A	0016491	molecular_function	oxidoreductase activity
A	0016668	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
A	0034599	biological_process	cellular response to oxidative stress
A	0045454	biological_process	cell redox homeostasis
A	0050660	molecular_function	flavin adenine dinucleotide binding
A	0050661	molecular_function	NADP binding
A	0070062	cellular_component	extracellular exosome
A	0098869	biological_process	cellular oxidant detoxification

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL A 3000

Chain	Residue
A	LEU54
A	GLN115
A	ARG127
A	HOH4179

site_id	AC2
Number of Residues	36
Details	BINDING SITE FOR RESIDUE FAD A 479

Chain	Residue
A	GLU50
A	SER51
A	HIS52
A	GLY56
A	THR57
A	CYS58
A	CYS63
A	LYS66
A	GLY128
A	HIS129
A	ALA130
A	ALA155
A	THR156
A	GLY157
A	TYR197
A	ARG291
A	ASN294
A	GLY330
A	ASP331
A	LEU337
A	LEU338
A	THR339
A	PRO340
A	HIS467
A	PRO468
A	HOH4060
A	HOH4068
A	HOH4069
A	HOH4072
A	HOH4126
A	HOH4138
A	GLY27
A	GLY29
A	SER30
A	GLY31
A	VAL49

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE AJ3 A 4058

Chain	Residue
A	SER30
A	ALA34
A	ARG37
A	GLY55
A	CYS58
A	VAL59
A	TYR114
A	ARG347

Functional Information from PROSITE/UniProt

site_id	PS00076
Number of Residues	11
Details	PYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGtCVnvGCVP

Chain	Residue	Details
A	GLY55-PRO65

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269\|PubMed:18638483, ECO:0000269\|PubMed:2585516, ECO:0000269\|PubMed:9546215, ECO:0007744\|PDB:1DNC, ECO:0007744\|PDB:1GRE, ECO:0007744\|PDB:1GSN, ECO:0007744\|PDB:3DK8

Chain	Residue	Details
A	VAL74

Chain	Residue	Details
A	HIS75
A	PHE94
A	GLU101
A	LEU110
A	GLY174
A	PRO375
A	THR383

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269\|PubMed:18638483, ECO:0000269\|PubMed:2585516, ECO:0000269\|PubMed:9546215, ECO:0007744\|PDB:1DNC, ECO:0007744\|PDB:1GRA, ECO:0007744\|PDB:1GRE, ECO:0007744\|PDB:1GSN

Chain	Residue	Details
A	ASP81

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269\|PubMed:16910673, ECO:0000269\|PubMed:18638483, ECO:0000269\|PubMed:2585516, ECO:0000269\|PubMed:3656429, ECO:0000269\|PubMed:8626496, ECO:0000269\|PubMed:9174360, ECO:0000269\|PubMed:9546215, ECO:0007744\|PDB:1BWC, ECO:0007744\|PDB:1GRA, ECO:0007744\|PDB:1GRG, ECO:0007744\|PDB:1GRT, ECO:0007744\|PDB:1K4Q, ECO:0007744\|PDB:2AAQ, ECO:0007744\|PDB:2GRT, ECO:0007744\|PDB:3DJJ, ECO:0007744\|PDB:3DK4, ECO:0007744\|PDB:3DK9, ECO:0007744\|PDB:3GRS, ECO:0007744\|PDB:3GRT, ECO:0007744\|PDB:3SQP, ECO:0007744\|PDB:5GRT

Chain	Residue	Details
A	LYS102

site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:18638483, ECO:0000269\|PubMed:2585516, ECO:0000269\|PubMed:9546215, ECO:0007744\|PDB:1DNC, ECO:0007744\|PDB:1GRA, ECO:0007744\|PDB:1GRE, ECO:0007744\|PDB:1GSN, ECO:0007744\|PDB:3DK4, ECO:0007744\|PDB:3DK8

Chain	Residue	Details
A	GLY158
A	TYR391

site_id	SWS_FT_FI6
Number of Residues	5
Details	BINDING: BINDING => ECO:0000269\|PubMed:18638483, ECO:0000269\|PubMed:2585516, ECO:0007744\|PDB:1GRB, ECO:0007744\|PDB:3DJG, ECO:0007744\|PDB:3DJJ

Chain	Residue	Details
A	GLU239
A	GLY242
A	GLU262
A	ALA268
A	GLY334

site_id	SWS_FT_FI7
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269\|PubMed:18638483, ECO:0000269\|PubMed:2585516, ECO:0007744\|PDB:3DJG, ECO:0007744\|PDB:3DJJ

Chain	Residue	Details
A	VAL245

site_id	SWS_FT_FI8
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269\|PubMed:18638483, ECO:0000269\|PubMed:2585516, ECO:0007744\|PDB:1GRB, ECO:0007744\|PDB:3DJG

Chain	Residue	Details
A	GLY381

site_id	SWS_FT_FI9
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269\|PubMed:18638483, ECO:0000269\|PubMed:2585516, ECO:0007744\|PDB:3DJG

Chain	Residue	Details
A	LYS414

site_id	SWS_FT_FI10
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:P47791

Chain	Residue	Details
A	ARG97

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1get

Chain	Residue	Details
A	HIS467
A	GLU472

site_id	CSA2
Number of Residues	5
Details	Annotated By Reference To The Literature 1get

Chain	Residue	Details
A	CYS58
A	GLU201
A	TYR197
A	LYS66
A	CYS63

site_id	MCSA1
Number of Residues	7
Details	M-CSA 6

Chain	Residue	Details
A	CYS58	electrofuge, electrophile, nucleofuge, nucleophile
A	CYS63	electrofuge, electrophile, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
A	LYS66	activator, electrostatic stabiliser, hydrogen bond donor
A	TYR197	activator
A	GLU201	activator, electrostatic stabiliser, hydrogen bond acceptor
A	HIS467	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	GLU472	activator, electrostatic stabiliser, hydrogen bond acceptor

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PDB entries from 2025-06-11

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