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	ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000305|PubMed:11121400

Chain	Residue	Details
A	GLU524

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site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250|UniProtKB:Q899Y1, ECO:0000303|PubMed:23703618

Chain	Residue	Details
A	GLU498
A	ALA531
A	VAL535
A	GLY537

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site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:21947205, ECO:0000269|PubMed:23703618, ECO:0007744|PDB:2Y50, ECO:0007744|PDB:2Y6I, ECO:0007744|PDB:4ARE

Chain	Residue	Details
A	HIS523
A	HIS527

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site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:21947205, ECO:0000269|PubMed:23703618, ECO:0007744|PDB:2Y50, ECO:0007744|PDB:2Y6I, ECO:0007744|PDB:4ARE

Chain	Residue	Details
A	GLU555

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