Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1QIN

HUMAN GLYOXALASE I COMPLEXED WITH S-(N-HYDROXY-N-P-IODOPHENYLCARBAMOYL) GLUTATHIONE

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 B 301

Chain	Residue
A	HIS126
A	GLU172
A	GIP300
B	GLN33
B	GLU99

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN A 401

Chain	Residue
A	GLN33
A	GLU99
B	HIS126
B	GLU172
B	GIP400

site_id	AC3
Number of Residues	27
Details	BINDING SITE FOR RESIDUE GIP A 300

Chain	Residue
A	ARG122
A	HIS126
A	LYS150
A	GLY155
A	LYS156
A	MET157
A	LEU160
A	PHE162
A	GLU172
A	MET179
A	MET183
A	HOH404
A	HOH435
A	HOH450
A	HOH462
A	HOH476
A	HOH491
A	HOH492
B	GLN33
B	ARG37
B	PHE67
B	LEU69
B	PHE71
B	GLU99
B	THR101
B	ASN103
B	ZN301

site_id	AC4
Number of Residues	26
Details	BINDING SITE FOR RESIDUE GIP B 400

Chain	Residue
B	GLU172
B	MET179
B	HOH413
B	HOH421
B	HOH422
B	HOH438
B	HOH448
B	HOH472
A	GLN33
A	ARG37
A	PHE67
A	LEU69
A	PHE71
A	GLU99
A	THR101
A	ASN103
A	ZN401
A	HOH406
B	ARG122
B	HIS126
B	LYS150
B	GLY155
B	LYS156
B	MET157
B	LEU160
B	PHE162

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

Chain	Residue
A	ZN401
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	ZN301
B	GLN33
B	GLU99
A	HIS126

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	292
Details	Domain: {"description":"VOC","evidences":[{"source":"PROSITE-ProRule","id":"PRU01163","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2
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	4
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	4
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Binding site: {"description":"in other chain"}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
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	2
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	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19199007","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	2
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	2
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9CPU0","evidenceCode":"ECO:0000250"}]}

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	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)