6AZP

A Structurally Dynamic N-terminal Region Drives Function of the Staphylococcal Peroxidase Inhibitor (SPIN)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004601	molecular_function	peroxidase activity
A	0006979	biological_process	response to oxidative stress
A	0020037	molecular_function	heme binding

Functional Information from PROSITE/UniProt

site_id	PS00435
Number of Residues	11
Details	PEROXIDASE_1 Peroxidases proximal heme-ligand signature. EMPELTSMHTL

Chain	Residue	Details
A	GLU408-LEU418

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton acceptor"}

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site_id	SWS_FT_FI2
Number of Residues	3
Details	Binding site: {"description":"covalent","evidences":[{"source":"PubMed","id":"23843990","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7840679","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CXP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EJX","evidenceCode":"ECO:0007744"}]}

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Residue

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site_id	SWS_FT_FI3
Number of Residues	1
Details	Binding site: {}

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site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10766826","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11705390","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7840679","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CXP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1D2V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1D7W","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1DNU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1DNW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1MHL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

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site_id	SWS_FT_FI5
Number of Residues	1
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"23843990","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7840679","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CXP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EJX","evidenceCode":"ECO:0007744"}]}

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site_id	SWS_FT_FI6
Number of Residues	1
Details	Site: {"description":"Transition state stabilizer"}

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site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Cysteine sulfenic acid (-SOH)","evidences":[{"source":"PubMed","id":"7840679","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI8
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16740002","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20332087","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI9
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20332087","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23843990","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4EJX","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI10
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","featureId":"CAR_000220","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16740002","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20332087","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23843990","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4EJX","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI11
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"20332087","evidenceCode":"ECO:0000269"}]}

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	2
Details	M-CSA 601

Chain	Residue	Details
A	HIS261	proton shuttle (general acid/base)
A	MET409	electrostatic stabiliser

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