Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1QIP

HUMAN GLYOXALASE I COMPLEXED WITH S-P-NITROBENZYLOXYCARBONYLGLUTATHIONE

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	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	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
C	0004462	molecular_function	lactoylglutathione lyase activity
C	0005515	molecular_function	protein binding
C	0005654	cellular_component	nucleoplasm
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0005886	cellular_component	plasma membrane
C	0005975	biological_process	carbohydrate metabolic process
C	0006749	biological_process	glutathione metabolic process
C	0008270	molecular_function	zinc ion binding
C	0009438	biological_process	methylglyoxal metabolic process
C	0016829	molecular_function	lyase activity
C	0030316	biological_process	osteoclast differentiation
C	0043066	biological_process	negative regulation of apoptotic process
C	0046872	molecular_function	metal ion binding
C	0070062	cellular_component	extracellular exosome
D	0004462	molecular_function	lactoylglutathione lyase activity
D	0005515	molecular_function	protein binding
D	0005654	cellular_component	nucleoplasm
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0005886	cellular_component	plasma membrane
D	0005975	biological_process	carbohydrate metabolic process
D	0006749	biological_process	glutathione metabolic process
D	0008270	molecular_function	zinc ion binding
D	0009438	biological_process	methylglyoxal metabolic process
D	0016829	molecular_function	lyase activity
D	0030316	biological_process	osteoclast differentiation
D	0043066	biological_process	negative regulation of apoptotic process
D	0046872	molecular_function	metal ion binding
D	0070062	cellular_component	extracellular exosome

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN B 901

Chain	Residue
A	HIS126
A	GLU172
A	HOH1227
A	HOH1228
B	GLN33
B	GLU99

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN A 902

Chain	Residue
B	HOH1225
A	GLN33
A	GLU99
A	HOH1229
B	HIS126
B	GLU172

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN D 903

Chain	Residue
C	HIS126
C	GLU172
C	HOH1232
D	GLN33
D	GLU99
D	HOH1227

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN C 904

Chain	Residue
C	GLN33
C	GLU99
C	HOH1233
D	HIS126
D	GLU172
D	HOH1228

site_id	AC5
Number of Residues	25
Details	BINDING SITE FOR RESIDUE GNB B 1001

Chain	Residue
A	ARG122
A	LEU160
A	PHE162
A	GLU172
A	MET179
A	LEU182
A	HOH1227
B	ARG37
B	CYS60
B	PHE67
B	ILE88
B	LEU92
B	THR101
B	ASN103
B	BME204
B	HOH1006
B	HOH1040
B	HOH1100
B	HOH1102
B	HOH1107
B	HOH1113
B	HOH1125
B	HOH1129
B	HOH1197
C	SER17

site_id	AC6
Number of Residues	22
Details	BINDING SITE FOR RESIDUE GNB A 1002

Chain	Residue
A	ARG37
A	GLN58
A	CYS60
A	PHE67
A	PHE71
A	ILE88
A	LEU92
A	THR101
A	ASN103
A	BME204
A	HOH1037
A	HOH1112
A	HOH1138
A	HOH1178
B	ARG122
B	MET157
B	LEU160
B	PHE162
B	TRP170
D	ASP154
D	LYS158
D	HOH1005

site_id	AC7
Number of Residues	25
Details	BINDING SITE FOR RESIDUE GNB D 1003

Chain	Residue
A	SER17
A	HOH1116
C	ARG122
C	MET157
C	LEU160
C	PHE162
C	MET179
C	HOH1061
D	ARG37
D	CYS60
D	PHE67
D	ILE88
D	LEU92
D	THR101
D	ASN103
D	BME204
D	HOH1049
D	HOH1104
D	HOH1105
D	HOH1109
D	HOH1114
D	HOH1117
D	HOH1125
D	HOH1128
D	HOH1194

site_id	AC8
Number of Residues	22
Details	BINDING SITE FOR RESIDUE GNB C 1004

Chain	Residue
C	ARG37
C	CYS60
C	PHE67
C	ILE88
C	LEU92
C	THR101
C	ASN103
C	BME204
C	HOH1005
C	HOH1038
C	HOH1092
C	HOH1109
C	HOH1113
C	HOH1165
C	HOH1171
C	HOH1186
C	HOH1225
D	ARG122
D	MET157
D	LEU160
D	PHE162
D	MET179

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE BME A 204

Chain	Residue
A	GLN58
A	LYS59
A	CYS60
A	PHE62
A	GNB1002

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE BME B 204

Chain	Residue
B	GLN58
B	LYS59
B	CYS60
B	LYS84
B	GNB1001
B	HOH1222

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE BME C 204

Chain	Residue
C	GLN58
C	CYS60
C	GNB1004

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE BME D 204

Chain	Residue
D	CYS60
D	PHE62
D	GNB1003

site_id	GH1
Number of Residues	3
Details	BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN2 HYD2 AND GSH2.

Chain	Residue
A	ARG37
A	ASN103
B	ARG122

site_id	GH2
Number of Residues	3
Details	BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN1 HYD1 AND GSH1.

Chain	Residue
B	ARG37
B	ASN103
A	ARG122

site_id	GH3
Number of Residues	3
Details	BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN2 HYD2 AND GSH2.

Chain	Residue
C	ARG37
C	ASN103
D	ARG122

site_id	GH4
Number of Residues	3
Details	BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN1 HYD1 AND GSH1.

Chain	Residue
D	ARG37
D	ASN103
C	ARG122

site_id	HD2
Number of Residues	14
Details	HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.

Chain	Residue
A	CYS60
A	PHE62
A	MET65
A	PHE67
A	LEU69
A	PHE71
A	ILE88
A	LEU92
B	MET157
B	LEU160
B	PHE162
B	LEU174
B	MET179
B	MET183

site_id	HD3
Number of Residues	14
Details	HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.

Chain	Residue
B	CYS60
B	PHE62
B	MET65
B	PHE67
B	LEU69
B	PHE71
B	ILE88
B	LEU92
A	MET157
A	LEU160
A	PHE162
A	LEU174
A	MET179
A	MET183

site_id	HD4
Number of Residues	14
Details	HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.

Chain	Residue
C	CYS60
C	PHE62
C	MET65
C	PHE67
C	LEU69
C	PHE71
C	ILE88
C	LEU92
D	MET157
D	LEU160
D	PHE162
D	LEU174
D	MET179
D	MET183

site_id	HD5
Number of Residues	14
Details	HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.

Chain	Residue
D	CYS60
D	PHE62
D	MET65
D	PHE67
D	LEU69
D	PHE71
D	ILE88
D	LEU92
C	MET157
C	LEU160
C	PHE162
C	LEU174
C	MET179
C	MET183

site_id	ZN1
Number of Residues	5
Details	ZINC BINDING SITE AT DIMER INTERFACE.

Chain	Residue
A	ZN902
A	GLN33
A	GLU99
B	HIS126
B	GLU172

site_id	ZN2
Number of Residues	5
Details	ZINC BINDING SITE AT DIMER INTERFACE.

Chain	Residue
A	GLU172
B	ZN901
B	GLN33
B	GLU99
A	HIS126

site_id	ZN3
Number of Residues	5
Details	ZINC BINDING SITE AT DIMER INTERFACE.

Chain	Residue
C	ZN904
C	GLN33
C	GLU99
D	HIS126
D	GLU172

site_id	ZN4
Number of Residues	5
Details	ZINC BINDING SITE AT DIMER INTERFACE.

Chain	Residue
D	ZN903
D	GLN33
D	GLU99
C	HIS126
C	GLU172

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	584
Details	Domain: {"description":"VOC","evidences":[{"source":"PROSITE-ProRule","id":"PRU01163","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"10521255","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9705294","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"23122816","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9218781","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9705294","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	8
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	8
Details	Binding site: {"description":"in other chain"}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	8
Details	Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"23122816","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9218781","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9705294","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	4
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9CPU0","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19199007","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	4
Details	Modified residue: {"description":"S-glutathionyl cysteine; alternate","evidences":[{"source":"PubMed","id":"20454679","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	4
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9CPU0","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	2
Details	Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"20454679","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25944712","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

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

Chain	Residue	Details
A	GLU172

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

Chain	Residue	Details
B	GLU172

site_id	CSA3
Number of Residues	1
Details	Annotated By Reference To The Literature 1fro

Chain	Residue	Details
C	GLU172

site_id	CSA4
Number of Residues	1
Details	Annotated By Reference To The Literature 1fro

Chain	Residue	Details
D	GLU172

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

site_id	MCSA3
Number of Residues	4
Details	M-CSA 32

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

site_id	MCSA4
Number of Residues	4
Details	M-CSA 32

Chain	Residue	Details
D	GLN33	metal ligand
D	GLU99	hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor
D	HIS126	metal ligand
D	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)