7OIH

Glycosylation in the crystal structure of neutrophil myeloperoxidase

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
E	0004601	molecular_function	peroxidase activity
E	0006979	biological_process	response to oxidative stress
E	0020037	molecular_function	heme binding
F	0004601	molecular_function	peroxidase activity
F	0006979	biological_process	response to oxidative stress
F	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

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	8
Details	ACT_SITE: Proton acceptor

Chain	Residue	Details
A	HIS261
B	HIS261
C	HIS261
D	HIS261
E	HIS261
F	HIS261
G	HIS261
H	HIS261

---

site_id	SWS_FT_FI2
Number of Residues	24
Details	BINDING: covalent => ECO:0000269|PubMed:23843990, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:4EJX

Chain	Residue	Details
A	ASP260
D	ASP260
D	GLU408
D	MET409
E	ASP260
E	GLU408
E	MET409
F	ASP260
F	GLU408
F	MET409
G	ASP260
A	GLU408
G	GLU408
G	MET409
H	ASP260
H	GLU408
H	MET409
A	MET409
B	ASP260
B	GLU408
B	MET409
C	ASP260
C	GLU408
C	MET409

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING:

Chain	Residue	Details
A	ASP262
B	ASP262
C	ASP262
D	ASP262
E	ASP262
F	ASP262
G	ASP262
H	ASP262

---

site_id	SWS_FT_FI4
Number of Residues	32
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
A	THR334
C	PHE336
C	ASP338
C	SER340
D	THR334
D	PHE336
D	ASP338
D	SER340
E	THR334
E	PHE336
E	ASP338
A	PHE336
E	SER340
F	THR334
F	PHE336
F	ASP338
F	SER340
G	THR334
G	PHE336
G	ASP338
G	SER340
H	THR334
A	ASP338
H	PHE336
H	ASP338
H	SER340
A	SER340
B	THR334
B	PHE336
B	ASP338
B	SER340
C	THR334

---

site_id	SWS_FT_FI5
Number of Residues	8
Details	BINDING: axial binding residue => ECO:0000269|PubMed:23843990, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:4EJX

Chain	Residue	Details
A	HIS502
B	HIS502
C	HIS502
D	HIS502
E	HIS502
F	HIS502
G	HIS502
H	HIS502

---

site_id	SWS_FT_FI6
Number of Residues	8
Details	SITE: Transition state stabilizer

Chain	Residue	Details
A	ARG405
B	ARG405
C	ARG405
D	ARG405
E	ARG405
F	ARG405
G	ARG405
H	ARG405

---

site_id	SWS_FT_FI7
Number of Residues	8
Details	MOD_RES: Cysteine sulfenic acid (-SOH) => ECO:0000269|PubMed:7840679

Chain	Residue	Details
A	CSO316
B	CSO316
C	CSO316
D	CSO316
E	CSO316
F	CSO316
G	CSO316
H	CSO316

---

site_id	SWS_FT_FI8
Number of Residues	8
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:20332087

Chain	Residue	Details
A	ASN323
B	ASN323
C	ASN323
D	ASN323
E	ASN323
F	ASN323
G	ASN323
H	ASN323

---

site_id	SWS_FT_FI9
Number of Residues	16
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
A	ASN355
E	ASN391
F	ASN355
F	ASN391
G	ASN355
G	ASN391
H	ASN355
H	ASN391
A	ASN391
B	ASN355
B	ASN391
C	ASN355
C	ASN391
D	ASN355
D	ASN391
E	ASN355

---

site_id	SWS_FT_FI10
Number of Residues	8
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
A	ASN483
B	ASN483
C	ASN483
D	ASN483
E	ASN483
F	ASN483
G	ASN483
H	ASN483

---

site_id	SWS_FT_FI11
Number of Residues	8
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:20332087

Chain	Residue	Details
A	ASN729
B	ASN729
C	ASN729
D	ASN729
E	ASN729
F	ASN729
G	ASN729
H	ASN729

---

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	ARG405	electrostatic stabiliser

---

site_id	MCSA2
Number of Residues	2
Details	M-CSA 601

Chain	Residue	Details
B	HIS261	proton shuttle (general acid/base)
B	ARG405	electrostatic stabiliser

---

site_id	MCSA3
Number of Residues	2
Details	M-CSA 601

Chain	Residue	Details
C	HIS261	proton shuttle (general acid/base)
C	ARG405	electrostatic stabiliser

---

site_id	MCSA4
Number of Residues	2
Details	M-CSA 601

Chain	Residue	Details
D	HIS261	proton shuttle (general acid/base)
D	ARG405	electrostatic stabiliser

---

site_id	MCSA5
Number of Residues	2
Details	M-CSA 601

Chain	Residue	Details
E	HIS261	proton shuttle (general acid/base)
E	ARG405	electrostatic stabiliser

---

site_id	MCSA6
Number of Residues	2
Details	M-CSA 601

Chain	Residue	Details
F	HIS261	proton shuttle (general acid/base)
F	ARG405	electrostatic stabiliser

---

site_id	MCSA7
Number of Residues	2
Details	M-CSA 601

Chain	Residue	Details
G	HIS261	proton shuttle (general acid/base)
G	ARG405	electrostatic stabiliser

---

site_id	MCSA8
Number of Residues	2
Details	M-CSA 601

Chain	Residue	Details
H	HIS261	proton shuttle (general acid/base)
H	ARG405	electrostatic stabiliser

---