3ZS1

Human Myeloperoxidase inactivated by TX5

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

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
C	GLU242-LEU252

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor

Chain	Residue	Details
C	MET190
D	MET190

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site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: covalent => ECO:0000269|PubMed:23843990, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:4EJX

Chain	Residue	Details
C	ASN189
C	THR337
C	LEU338
D	ASN189
D	THR337
D	LEU338

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site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING:

Chain	Residue	Details
C	SER191
D	SER191

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site_id	SWS_FT_FI4
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:10766826, ECO:0000269|PubMed:11705390, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:1D2V, ECO:0007744|PDB:1D7W, ECO:0007744|PDB:1DNU, ECO:0007744|PDB:1DNW, ECO:0007744|PDB:1MHL

Chain	Residue	Details
C	GLU263
C	LYS265
C	LEU267
C	PRO269
D	GLU263
D	LYS265
D	LEU267
D	PRO269

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site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: axial binding residue => ECO:0000269|PubMed:23843990, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:4EJX

Chain	Residue	Details
C	PRO431
D	PRO431

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site_id	SWS_FT_FI6
Number of Residues	2
Details	SITE: Transition state stabilizer

Chain	Residue	Details
C	TYR334
D	TYR334

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site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Cysteine sulfenic acid (-SOH) => ECO:0000269|PubMed:7840679

Chain	Residue	Details
C	GLU245
D	GLU245

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site_id	SWS_FT_FI8
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:20332087

Chain	Residue	Details
C	LEU252
D	LEU252

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site_id	SWS_FT_FI9
Number of Residues	4
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20332087, ECO:0000269|PubMed:23843990, ECO:0007744|PDB:4EJX

Chain	Residue	Details
C	VAL284
C	VAL320
D	VAL284
D	VAL320

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site_id	SWS_FT_FI10
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:20332087, ECO:0000269|PubMed:23843990, ECO:0007744|PDB:4EJX

Chain	Residue	Details
C	ARG412
D	ARG412

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	2
Details	M-CSA 601

Chain	Residue	Details
C	MET190	proton shuttle (general acid/base)
C	TYR334	electrostatic stabiliser

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site_id	MCSA2
Number of Residues	2
Details	M-CSA 601

Chain	Residue	Details
D	MET190	proton shuttle (general acid/base)
D	TYR334	electrostatic stabiliser

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