7Z5U

Crystal structure of the peptidase domain of collagenase G from Clostridium histolyticum in complex with a hydroxamate-based inhibitor

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 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

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
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

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site_id	SWS_FT_FI2
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

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site_id	SWS_FT_FI3
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

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site_id	SWS_FT_FI4
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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