3FKG

Crystal Structure Analysis of Fungal Versatile Peroxidase from Pleurotus eryngii

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	0016491	molecular_function	oxidoreductase activity
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	25
Details	BINDING SITE FOR RESIDUE HEM A 350

Chain	Residue
A	HIS39
A	LEU166
A	SER168
A	HIS169
A	ALA172
A	ALA173
A	ALA174
A	ASP175
A	LYS176
A	VAL177
A	LEU228
A	GLU40
A	SER230
A	ZN337
A	HOH372
A	HOH458
A	HOH512
A	HOH595
A	LEU42
A	ARG43
A	PHE46
A	PRO139
A	GLU140
A	PRO141
A	LEU165

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 351

Chain	Residue
A	ASP48
A	GLY60
A	ASP62
A	SER64
A	HOH373
A	HOH441

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 352

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

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN A 332

Chain	Residue
A	ASP30
A	GLU37
A	HIS232
A	ARG236
A	HOH404

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 333

Chain	Residue
A	GLU26
A	ASP237
A	HOH405
A	HOH406

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 334

Chain	Residue
A	GLU140
A	ASP143
A	CAC342
A	CAC343

---

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE A 335

Chain	Residue
A	HIS293
A	ASP318
A	HOH408
A	HOH409

---

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 336

Chain	Residue
A	HIS95
A	HOH410
A	HOH411
A	HOH412

---

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN A 337

Chain	Residue
A	ASP175
A	FE340
A	HEM350

---

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN A 338

Chain	Residue
A	HIS136
A	GLU140
A	CAC342
A	CAC343
A	HOH413

---

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 339

Chain	Residue
A	GLU36
A	GLU40
A	GLU83
A	FE340

---

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FE A 340

Chain	Residue
A	GLU40
A	GLU83
A	ASP175
A	ZN337
A	ZN339
A	HOH414

---

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE A 341

Chain	Residue
A	ASP69
A	LYS89
A	HOH415
A	HOH416
A	HOH417

---

site_id	BC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE CAC A 342

Chain	Residue
A	HIS136
A	VAL138
A	GLU140
A	ASP143
A	ZN334
A	ZN338
A	CAC343
A	HOH413
A	HOH418
A	HOH461

---

site_id	BC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE CAC A 343

Chain	Residue
A	HOH484
A	HOH663
A	HIS136
A	GLU140
A	PHE142
A	ASP143
A	ZN334
A	ZN338
A	CAC342
A	HOH374
A	HOH413

---

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	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00297","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10012","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Tryptophan radical intermediate","evidences":[{"source":"PubMed","id":"16246366","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16246366","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	13
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Binding site: {"description":"axial binding residue"}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Site: {"description":"Transition state stabilizer","evidences":[{"source":"PROSITE-ProRule","id":"PRU00297","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1apx

Chain	Residue	Details
A	HIS47
A	ARG43
A	ASN78

---