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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3DJG

Catalytic cycle of human glutathione reductase near 1 A resolution

Functional Information from GO Data

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	37
Details	BINDING SITE FOR RESIDUE FAD X 479

Chain	Residue
X	GLY27
X	CYS58
X	GLY62
X	CYS63
X	LYS66
X	GLY128
X	HIS129
X	ALA130
X	ALA155
X	THR156
X	GLY157
X	GLY29
X	ARG291
X	LEU298
X	GLY330
X	ASP331
X	LEU337
X	LEU338
X	THR339
X	PRO340
X	HIS467
X	PRO468
X	SER30
X	HOH485
X	HOH487
X	HOH493
X	HOH498
X	HOH534
X	HOH795
X	HOH827
X	HOH832
X	GLY31
X	GLU50
X	SER51
X	HIS52
X	GLY56
X	THR57

site_id	AC2
Number of Residues	28
Details	BINDING SITE FOR RESIDUE NDP X 483

Chain	Residue
X	LYS66
X	ALA195
X	GLY196
X	TYR197
X	ILE198
X	GLU201
X	ARG218
X	HIS219
X	ARG224
X	ILE289
X	GLY290
X	ARG291
X	LEU337
X	LEU338
X	PHE372
X	HOH507
X	HOH510
X	HOH520
X	HOH535
X	HOH568
X	HOH592
X	HOH797
X	HOH839
X	HOH840
X	HOH853
X	HOH939
X	HOH990
X	HOH998

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
X	GLY55-PRO65

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000269\|PubMed:16910673, ECO:0000269\|PubMed:18638483, ECO:0007744\|PDB:2GH5

Chain	Residue	Details
X	HIS467

site_id	SWS_FT_FI2
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
X	SER30

Chain	Residue	Details
X	GLY31
X	GLU50
X	THR57
X	LYS66
X	ALA130
X	ASP331
X	THR339

site_id	SWS_FT_FI4
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
X	ARG37

site_id	SWS_FT_FI5
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
X	CYS58

site_id	SWS_FT_FI6
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
X	TYR114
X	ARG347

site_id	SWS_FT_FI7
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
X	ALA195
X	ILE198
X	ARG218
X	ARG224
X	GLY290

site_id	SWS_FT_FI8
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
X	GLU201

site_id	SWS_FT_FI9
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
X	LEU337

site_id	SWS_FT_FI10
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269\|PubMed:18638483, ECO:0000269\|PubMed:2585516, ECO:0007744\|PDB:3DJG

Chain	Residue	Details
X	VAL370

site_id	SWS_FT_FI11
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:1DNC, ECO:0007744\|PDB:1GRA, ECO:0007744\|PDB:1GRB, ECO:0007744\|PDB:1GRE, ECO:0007744\|PDB:1GRF, ECO:0007744\|PDB:1GRG, ECO:0007744\|PDB:1GRH, ECO:0007744\|PDB:1GRT, ECO:0007744\|PDB:1GSN, ECO:0007744\|PDB:1K4Q, ECO:0007744\|PDB:1XAN, ECO:0007744\|PDB:2AAQ, ECO:0007744\|PDB:2GH5, ECO:0007744\|PDB:2GRT, ECO:0007744\|PDB:3DJG, ECO:0007744\|PDB:3DJJ, ECO:0007744\|PDB:3DK4, ECO:0007744\|PDB:3DK8, ECO:0007744\|PDB:3DK9, ECO:0007744\|PDB:3GRS, ECO:0007744\|PDB:3SQP, ECO:0007744\|PDB:4GR1, ECO:0007744\|PDB:5GRT

Chain	Residue	Details
X	HIS467

site_id	SWS_FT_FI12
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:P47791

Chain	Residue	Details
X	LYS53

Catalytic Information from CSA

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

Chain	Residue	Details
X	CYS58
X	CYS63

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1get

Chain	Residue	Details
X	HIS467
X	GLU472

site_id	MCSA1
Number of Residues	7
Details	M-CSA 6

Chain

Residue

Details

237992

PDB entries from 2025-06-25

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