5WDJ

CRYSTAL STRUCTURE OF MYELOPEROXIDASE SUBFORM C (MPO) COMPLEX WITH COMPOUND-6 AKA 7-(BENZYLOXY)-1H-[1,2, 3]TRIAZOLO[4,5-D]PYRIMIDIN-5-AMINE

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
D	0004601	molecular_function	peroxidase activity
D	0006979	biological_process	response to oxidative stress
D	0020037	molecular_function	heme binding
E	0004601	molecular_function	peroxidase activity
E	0006979	biological_process	response to oxidative stress
E	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	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
B	MET190
E	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
B	ASN189
B	THR337
B	LEU338
E	ASN189
E	THR337
E	LEU338

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site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING:

Chain	Residue	Details
B	SER191
E	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
B	GLU263
B	LYS265
B	LEU267
B	PRO269
E	GLU263
E	LYS265
E	LEU267
E	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
B	PRO431
E	PRO431

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

Chain	Residue	Details
B	TYR334
E	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
B	GLU245
E	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
B	LEU252
E	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
B	VAL284
B	VAL320
E	VAL284
E	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
B	ARG412
E	ARG412

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	2
Details	M-CSA 601

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

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site_id	MCSA2
Number of Residues	2
Details	M-CSA 601

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

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