Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7Z53

Structure of native leukocyte myeloperoxidase in complex with a truncated version (SPIN truncated) of the Staphyloccal Peroxidase Inhibitor SPIN from Staphylococcus aureus

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
B	0004601	molecular_function	peroxidase activity
B	0006979	biological_process	response to oxidative stress
B	0020037	molecular_function	heme binding
C	0004601	molecular_function	peroxidase activity
C	0006979	biological_process	response to oxidative stress
C	0020037	molecular_function	heme binding
D	0004601	molecular_function	peroxidase activity
D	0006979	biological_process	response to oxidative stress
D	0020037	molecular_function	heme binding
G	0004601	molecular_function	peroxidase activity
G	0006979	biological_process	response to oxidative stress
G	0020037	molecular_function	heme binding
H	0004601	molecular_function	peroxidase activity
H	0006979	biological_process	response to oxidative stress
H	0020037	molecular_function	heme binding
I	0004601	molecular_function	peroxidase activity
I	0006979	biological_process	response to oxidative stress
I	0020037	molecular_function	heme binding
J	0004601	molecular_function	peroxidase activity
J	0006979	biological_process	response to oxidative stress
J	0020037	molecular_function	heme binding
M	0004601	molecular_function	peroxidase activity
M	0006979	biological_process	response to oxidative stress
M	0020037	molecular_function	heme binding
N	0004601	molecular_function	peroxidase activity
N	0006979	biological_process	response to oxidative stress
N	0020037	molecular_function	heme binding
O	0004601	molecular_function	peroxidase activity
O	0006979	biological_process	response to oxidative stress
O	0020037	molecular_function	heme binding
P	0004601	molecular_function	peroxidase activity
P	0006979	biological_process	response to oxidative stress
P	0020037	molecular_function	heme binding
S	0004601	molecular_function	peroxidase activity
S	0006979	biological_process	response to oxidative stress
S	0020037	molecular_function	heme binding
T	0004601	molecular_function	peroxidase activity
T	0006979	biological_process	response to oxidative stress
T	0020037	molecular_function	heme binding
U	0004601	molecular_function	peroxidase activity
U	0006979	biological_process	response to oxidative stress
U	0020037	molecular_function	heme binding
V	0004601	molecular_function	peroxidase activity
V	0006979	biological_process	response to oxidative stress
V	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
B	GLU408-LEU418

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Active site: {"description":"Proton acceptor"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	24
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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	32
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

Details

site_id	SWS_FT_FI5
Number of Residues	8
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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	8
Details	Site: {"description":"Transition state stabilizer"}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	8
Details	Modified residue: {"description":"Cysteine sulfenic acid (-SOH)","evidences":[{"source":"PubMed","id":"7840679","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	8
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

site_id	SWS_FT_FI9
Number of Residues	16
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

site_id	SWS_FT_FI10
Number of Residues	8
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

site_id	SWS_FT_FI11
Number of Residues	8
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"20332087","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	1
Details	M-CSA 601

Chain	Residue	Details
B	MET409	electrostatic stabiliser

site_id	MCSA2
Number of Residues	1
Details	M-CSA 601

Chain	Residue	Details
D	MET409	electrostatic stabiliser

site_id	MCSA3
Number of Residues	1
Details	M-CSA 601

Chain	Residue	Details
H	MET409	electrostatic stabiliser

site_id	MCSA4
Number of Residues	1
Details	M-CSA 601

Chain	Residue	Details
J	MET409	electrostatic stabiliser

site_id	MCSA5
Number of Residues	1
Details	M-CSA 601

Chain	Residue	Details
N	MET409	electrostatic stabiliser

site_id	MCSA6
Number of Residues	1
Details	M-CSA 601

Chain	Residue	Details
P	MET409	electrostatic stabiliser

site_id	MCSA7
Number of Residues	1
Details	M-CSA 601

Chain	Residue	Details
T	MET409	electrostatic stabiliser

site_id	MCSA8
Number of Residues	1
Details	M-CSA 601

Chain	Residue	Details
V	MET409	electrostatic stabiliser

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)