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	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

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	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	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

---