4FCN

The crystal structures of several mutants of pleurotus eryngii versatile peroxidase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000302	biological_process	response to reactive oxygen species
A	0004601	molecular_function	peroxidase activity
A	0005576	cellular_component	extracellular region
A	0006979	biological_process	response to oxidative stress
A	0016689	molecular_function	manganese peroxidase activity
A	0020037	molecular_function	heme binding
A	0034599	biological_process	cellular response to oxidative stress
A	0042744	biological_process	hydrogen peroxide catabolic process
A	0046274	biological_process	lignin catabolic process
A	0046872	molecular_function	metal ion binding
A	0052750	molecular_function	reactive-black-5:hydrogen-peroxide oxidoreductase activity
A	0098869	biological_process	cellular oxidant detoxification

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 401

Chain	Residue
A	SER170
A	ASP187
A	THR189
A	VAL192
A	ASP194

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 402

Chain	Residue
A	HOH520
A	HOH548
A	ASP48
A	GLY60
A	ASP62
A	SER64

---

site_id	AC3
Number of Residues	26
Details	BINDING SITE FOR RESIDUE HEM A 403

Chain	Residue
A	GLU36
A	HIS39
A	GLU40
A	LEU42
A	ARG43
A	PHE46
A	GLY140
A	PRO141
A	LEU165
A	LEU166
A	SER168
A	HIS169
A	ALA172
A	ALA173
A	ALA174
A	ASP175
A	GLY176
A	VAL177
A	PHE186
A	LEU228
A	SER230
A	HOH597
A	HOH623
A	HOH645
A	HOH649
A	HOH734

---

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SO4 A 404

Chain	Residue
A	HIS136
A	PHE142
A	ARG206
A	HOH565
A	HOH577
A	HOH754
A	HOH763
A	HOH802
A	HOH840
A	HOH841

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	GLU161-ILE171

---

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

Chain	Residue	Details
A	VAL38-ALA49

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000255|PROSITE-ProRule:PRU10012

Chain	Residue	Details
A	HIS47

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Tryptophan radical intermediate => ECO:0000269|PubMed:16246366

Chain	Residue	Details
A	TRP164

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:16246366

Chain	Residue	Details
A	GLU36
A	ASP175

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	GLU40

---

site_id	SWS_FT_FI5
Number of Residues	10
Details	BINDING:

Chain	Residue	Details
A	ASP48
A	ASP194
A	GLY60
A	ASP62
A	SER64
A	SER170
A	ALA173
A	ASP187
A	THR189
A	VAL192

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	BINDING: axial binding residue

Chain	Residue	Details
A	HIS169

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	SITE: Transition state stabilizer => ECO:0000255|PROSITE-ProRule:PRU00297

Chain	Residue	Details
A	ARG43

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN96

---