4ARE

Crystal structure of the collagenase Unit of collagenase G from Clostridium histolyticum at 2.19 angstrom resolution.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004222	molecular_function	metalloendopeptidase activity
A	0005576	cellular_component	extracellular region
A	0006508	biological_process	proteolysis
A	0008270	molecular_function	zinc ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN A 1790

Chain	Residue
A	HIS523
A	GLU524
A	HIS527
A	GLU555
A	HOH2168
A	HOH2169

---

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE P6G A 1791

Chain	Residue
A	TRP337
A	ASP340
A	TYR344
A	HOH2267
A	PRO278
A	ASP279
A	TYR280

---

site_id	AC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE FLC A 1792

Chain	Residue
A	SER568
A	VAL570
A	TYR618
A	GLU619
A	MET622
A	TRP736
A	ASP737
A	LYS741
A	HOH2117
A	HOH2196
A	HOH2251

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE TRS A 1793

Chain	Residue
A	TYR344
A	LYS348
A	ARG382
A	TRP385
A	HOH2269

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU520-LEU529

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	269
Details	Region: {"description":"Activator domain required for full activity on collagen","evidences":[{"source":"PubMed","id":"21947205","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23703618","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	281
Details	Region: {"description":"Catalytic subdomain","evidences":[{"source":"PubMed","id":"23703618","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11121400","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q899Y1","evidenceCode":"ECO:0000250"},{"source":"PubMed","id":"23703618","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21947205","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23703618","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2Y50","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2Y6I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ARE","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21947205","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23703618","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2Y50","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2Y6I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ARE","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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