1QIB

CRYSTAL STRUCTURE OF GELATINASE A CATALYTIC DOMAIN

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004222	molecular_function	metalloendopeptidase activity
A	0006508	biological_process	proteolysis
A	0008237	molecular_function	metallopeptidase activity
A	0008270	molecular_function	zinc ion binding
A	0031012	cellular_component	extracellular matrix

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN A 501

Chain	Residue
A	HIS201
A	HIS205
A	HIS211

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 502

Chain	Residue
A	HIS151
A	ASP153
A	HIS166
A	HIS179

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site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 503

Chain	Residue
A	ASP161
A	LEU163
A	ASP181
A	GLU184
A	ASP158
A	GLY159

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site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 504

Chain	Residue
A	ASP141
A	GLY173
A	GLY175
A	ASP177
A	HOH303
A	HOH304

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site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 505

Chain	Residue
A	ASP107
A	ASP182
A	GLU184
A	HOH301
A	HOH302

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Functional Information from PROSITE/UniProt

site_id	PS00142
Number of Residues	10
Details	ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VAAHEFGHAM

Chain	Residue	Details
A	VAL198-MET207

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000305|PubMed:10356396

Chain	Residue	Details
A	GLU202

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:21813640, ECO:0007744|PDB:1QIB, ECO:0007744|PDB:3AYU

Chain	Residue	Details
A	ASP107
A	ASP182

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:21813640, ECO:0007744|PDB:1EAK, ECO:0007744|PDB:3AYU

Chain	Residue	Details
A	ASP141
A	GLY173

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:10356396, ECO:0000269|PubMed:12032297, ECO:0000269|PubMed:21813640, ECO:0007744|PDB:1CK7, ECO:0007744|PDB:1EAK, ECO:0007744|PDB:1GXD, ECO:0007744|PDB:1QIB, ECO:0007744|PDB:3AYU

Chain	Residue	Details
A	HIS151
A	ASP153
A	HIS166
A	HIS179

---

site_id	SWS_FT_FI5
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:21813640, ECO:0007744|PDB:3AYU

Chain	Residue	Details
A	ASP158
A	GLY159
A	GLY175
A	ASP177
A	ASP181
A	GLU184

---

site_id	SWS_FT_FI6
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:10356396, ECO:0000269|PubMed:12032297, ECO:0000269|PubMed:21813640, ECO:0007744|PDB:1CK7, ECO:0007744|PDB:1EAK, ECO:0007744|PDB:1GXD, ECO:0007744|PDB:3AYU

Chain	Residue	Details
A	HIS201
A	HIS205
A	HIS211

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	a catalytic site defined by CSA, PubMed 12401069

Chain	Residue	Details
A	GLU202

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site_id	MCSA1
Number of Residues	4
Details	M-CSA 906

Chain	Residue	Details
A	HIS201	metal ligand
A	GLU202	proton shuttle (general acid/base)
A	HIS205	metal ligand
A	HIS211	metal ligand

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