1GW2

RECOMBINANT HORSERADISH PEROXIDASE C1A THR171SER IN COMPLEX WITH FERULIC ACID

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004601	molecular_function	peroxidase activity
A	0005576	cellular_component	extracellular region
A	0005773	cellular_component	vacuole
A	0006979	biological_process	response to oxidative stress
A	0020037	molecular_function	heme binding
A	0042744	biological_process	hydrogen peroxide catabolic process
A	0046872	molecular_function	metal ion binding
A	0098869	biological_process	cellular oxidant detoxification
A	0140825	molecular_function	lactoperoxidase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 501

Chain	Residue
A	ASP43
A	VAL46
A	GLY48
A	ASP50
A	SER52
A	HOH2114

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 502

Chain	Residue
A	ILE228
A	ASP230
A	SER171
A	ASP222
A	THR225

---

site_id	AC3
Number of Residues	27
Details	BINDING SITE FOR RESIDUE HEM A 350

Chain	Residue
A	ARG31
A	ALA34
A	SER35
A	ARG38
A	PHE41
A	SER73
A	ARG75
A	PRO139
A	ALA140
A	PRO141
A	PHE152
A	LEU163
A	LEU166
A	GLY169
A	HIS170
A	PHE172
A	GLY173
A	LYS174
A	ASN175
A	GLN176
A	PHE179
A	PHE221
A	SER246
A	FER601
A	HOH2243
A	HOH2385
A	HOH2386

---

site_id	AC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE FER A 601

Chain	Residue
A	ARG38
A	HIS42
A	PHE68
A	GLY69
A	SER73
A	PRO139
A	ALA140
A	PHE179
A	HEM350
A	HOH2387
A	HOH2388

---

site_id	AC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE FER A 602

Chain	Residue
A	ASN16
A	ILE17
A	ASP20
A	ALA90
A	ARG224
A	LYS232
A	HOH2026
A	HOH2154
A	HOH2167
A	HOH2389

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ASP162-PHE172

---

site_id	PS00436
Number of Residues	12
Details	PEROXIDASE_2 Peroxidases active site signature. AAsiLRLhFHDC

Chain	Residue	Details
A	ALA33-CYS44

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor

Chain	Residue	Details
A	HIS42

---

site_id	SWS_FT_FI2
Number of Residues	11
Details	BINDING:

Chain	Residue	Details
A	ASP43
A	THR225
A	ASP230
A	VAL46
A	GLY48
A	ASP50
A	SER52
A	GLU64
A	PRO139
A	SER171
A	ASP222

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: axial binding residue

Chain	Residue	Details
A	HIS170

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	SITE: Transition state stabilizer

Chain	Residue	Details
A	ARG38

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Pyrrolidone carboxylic acid => ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000269|PubMed:1001465

Chain	Residue	Details
A	GLN1

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:1001465

Chain	Residue	Details
A	ASN13
A	ASN57

---

site_id	SWS_FT_FI7
Number of Residues	6
Details	CARBOHYD: N-linked (GlcNAc...) asparagine

Chain	Residue	Details
A	ASN158
A	ASN186
A	ASN198
A	ASN214
A	ASN255
A	ASN268

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 7atj

Chain	Residue	Details
A	ARG38
A	HIS42
A	ASN70

---

site_id	MCSA1
Number of Residues	4
Details	M-CSA 239

Chain	Residue	Details
A	ARG38	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	HIS42	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	ASN70	electrostatic stabiliser, hydrogen bond acceptor, increase acidity, increase basicity
A	HIS170	metal ligand

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