Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3VW9

Human Glyoxalase I with an N-hydroxypyridone inhibitor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004462	molecular_function	lactoylglutathione lyase activity
A	0005515	molecular_function	protein binding
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0005975	biological_process	carbohydrate metabolic process
A	0006357	biological_process	regulation of transcription by RNA polymerase II
A	0006749	biological_process	glutathione metabolic process
A	0008270	molecular_function	zinc ion binding
A	0009438	biological_process	methylglyoxal metabolic process
A	0016829	molecular_function	lyase activity
A	0030316	biological_process	osteoclast differentiation
A	0043066	biological_process	negative regulation of apoptotic process
A	0046872	molecular_function	metal ion binding
A	0070062	cellular_component	extracellular exosome
B	0004462	molecular_function	lactoylglutathione lyase activity
B	0005515	molecular_function	protein binding
B	0005654	cellular_component	nucleoplasm
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0005975	biological_process	carbohydrate metabolic process
B	0006357	biological_process	regulation of transcription by RNA polymerase II
B	0006749	biological_process	glutathione metabolic process
B	0008270	molecular_function	zinc ion binding
B	0009438	biological_process	methylglyoxal metabolic process
B	0016829	molecular_function	lyase activity
B	0030316	biological_process	osteoclast differentiation
B	0043066	biological_process	negative regulation of apoptotic process
B	0046872	molecular_function	metal ion binding
B	0070062	cellular_component	extracellular exosome

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN A 201

Chain	Residue
A	GLN33
A	GLU99
B	HIS126
B	GLU172
B	HPJ202

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EPE A 202

Chain	Residue
A	HOH454
A	HOH465
A	SER20
A	ASP21
A	ASP153
A	LYS178

site_id	AC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE HPJ A 203

Chain	Residue
A	HIS126
A	MET157
A	PHE162
A	GLU172
A	MET179
A	MET183
A	HOH336
B	GLN33
B	CYS60
B	MET65
B	LEU69
B	GLU99
B	ZN201

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN B 201

Chain	Residue
A	HIS126
A	GLU172
A	HPJ203
B	GLN33
B	GLU99

site_id	AC5
Number of Residues	14
Details	BINDING SITE FOR RESIDUE HPJ B 202

Chain	Residue
A	GLN33
A	CYS60
A	LEU92
A	GLU99
A	ZN201
B	SER17
B	HIS126
B	MET157
B	PHE162
B	GLU172
B	MET179
B	ALA180
B	HOH1066
B	HOH1182

Functional Information from PROSITE/UniProt

site_id	PS00934
Number of Residues	22
Details	GLYOXALASE_I_1 Glyoxalase I signature 1. QTmLrVkdpkKSldFYtrvLGM

Chain	Residue	Details
A	GLN33-MET54

site_id	PS00935
Number of Residues	17
Details	GLYOXALASE_I_2 Glyoxalase I signature 2. GNsdpr.GFGHIGiAvpD

Chain	Residue	Details
A	GLY117-ASP133

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton donor/acceptor => ECO:0000269\|PubMed:10521255, ECO:0000269\|PubMed:9705294

Chain	Residue	Details
A	GLU172
B	GLU172

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:23122816, ECO:0000269\|PubMed:9218781, ECO:0000269\|PubMed:9705294

Chain	Residue	Details
A	GLN33
A	GLU99
B	GLN33
B	GLU99

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING:

Chain	Residue	Details
B	ARG37
B	ASN103
A	ARG37
A	ASN103

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: in other chain

Chain	Residue	Details
B	ARG122
B	LYS156
A	ARG122
A	LYS156

site_id	SWS_FT_FI5
Number of Residues	4
Details	BINDING: in other chain => ECO:0000269\|PubMed:23122816, ECO:0000269\|PubMed:9218781, ECO:0000269\|PubMed:9705294

Chain	Residue	Details
A	HIS126
A	GLU172
B	HIS126
B	GLU172

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: N-acetylalanine => ECO:0000269\|PubMed:20454679, ECO:0007744\|PubMed:19413330, ECO:0007744\|PubMed:25944712

Chain	Residue	Details
A	ALA1
B	ALA1

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: N6-succinyllysine => ECO:0000250\|UniProtKB:Q9CPU0

Chain	Residue	Details
A	LYS87
B	LYS87

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0000269\|PubMed:19199007

Chain	Residue	Details
A	THR106
B	THR106

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: S-glutathionyl cysteine; alternate => ECO:0000269\|PubMed:20454679

Chain	Residue	Details
A	CYS138
B	CYS138

site_id	SWS_FT_FI10
Number of Residues	2
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250\|UniProtKB:Q9CPU0

Chain	Residue	Details
A	LYS147
B	LYS147

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 32

Chain	Residue	Details
A	GLN33	metal ligand
A	GLU99	hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor
A	HIS126	metal ligand
A	GLU172	hydrogen bond acceptor, metal ligand, proton acceptor, proton donor, proton relay

site_id	MCSA2
Number of Residues	4
Details	M-CSA 32

Chain	Residue	Details
B	GLN33	metal ligand
B	GLU99	hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor
B	HIS126	metal ligand
B	GLU172	hydrogen bond acceptor, metal ligand, proton acceptor, proton donor, proton relay

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)