7SKM

Complex between S. aureus aureolysin and wt IMPI.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004222	molecular_function	metalloendopeptidase activity
A	0006508	biological_process	proteolysis
C	0004222	molecular_function	metalloendopeptidase activity
C	0006508	biological_process	proteolysis

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	VAL349-VAL358

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site_id	PS01186
Number of Residues	15
Details	EGF_2 EGF-like domain signature 2. CyCedGYardvngk.C

Chain	Residue	Details
E	CYS63-CYS77

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"evidences":[{"source":"PubMed","id":"9753696","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Proton donor"}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	26
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9753696","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BQB","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"9738891","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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