4W7J

CRYSTAL STRUCTURE OF A DECOLORIZING PEROXIDASE (DYP) FROM AURICULARIA AURICULA-JUDAE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004601	molecular_function	peroxidase activity
A	0005576	cellular_component	extracellular region
A	0005829	cellular_component	cytosol
A	0020037	molecular_function	heme binding
A	0046872	molecular_function	metal ion binding
A	0098869	biological_process	cellular oxidant detoxification
A	0140825	molecular_function	lactoperoxidase activity
B	0004601	molecular_function	peroxidase activity
B	0005576	cellular_component	extracellular region
B	0005829	cellular_component	cytosol
B	0020037	molecular_function	heme binding
B	0046872	molecular_function	metal ion binding
B	0098869	biological_process	cellular oxidant detoxification
B	0140825	molecular_function	lactoperoxidase activity
C	0004601	molecular_function	peroxidase activity
C	0005576	cellular_component	extracellular region
C	0005829	cellular_component	cytosol
C	0020037	molecular_function	heme binding
C	0046872	molecular_function	metal ion binding
C	0098869	biological_process	cellular oxidant detoxification
C	0140825	molecular_function	lactoperoxidase activity
D	0004601	molecular_function	peroxidase activity
D	0005576	cellular_component	extracellular region
D	0005829	cellular_component	cytosol
D	0020037	molecular_function	heme binding
D	0046872	molecular_function	metal ion binding
D	0098869	biological_process	cellular oxidant detoxification
D	0140825	molecular_function	lactoperoxidase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	25
Details	binding site for residue HEM A 501

Chain	Residue
A	GLU162
A	ARG255
A	HIS304
A	ILE305
A	THR308
A	ARG309
A	ARG311
A	ARG332
A	PHE359
A	PHE370
A	ILE398
A	PHE166
A	VAL426
A	HOH641
A	HOH646
A	HOH658
A	HOH667
A	HOH676
A	LEU167
A	ASP168
A	GLY169
A	ILE170
A	ALA171
A	GLN221
A	VAL253

---

site_id	AC2
Number of Residues	23
Details	binding site for residue HEM B 501

Chain	Residue
B	GLU162
B	PHE166
B	LEU167
B	ASP168
B	GLY169
B	ILE170
B	ALA171
B	GLN221
B	ARG255
B	HIS304
B	ILE305
B	THR308
B	ARG309
B	ARG311
B	ARG332
B	PHE359
B	PHE370
B	ILE398
B	HOH677
B	HOH679
B	HOH711
B	HOH729
B	HOH743

---

site_id	AC3
Number of Residues	24
Details	binding site for residue HEM C 501

Chain	Residue
C	GLU162
C	PHE166
C	LEU167
C	ASP168
C	GLY169
C	ILE170
C	ALA171
C	GLN221
C	ARG255
C	HIS304
C	ILE305
C	THR308
C	ARG309
C	ARG311
C	ARG332
C	PHE359
C	PHE370
C	GLN374
C	ILE398
C	HOH669
C	HOH674
C	HOH685
C	HOH705
C	HOH753

---

site_id	AC4
Number of Residues	23
Details	binding site for residue HEM D 501

Chain	Residue
D	GLU162
D	PHE166
D	LEU167
D	GLY169
D	ILE170
D	ALA171
D	GLN221
D	ARG255
D	HIS304
D	ILE305
D	THR308
D	ARG309
D	ARG311
D	ARG332
D	PHE359
D	PHE370
D	GLN374
D	ILE398
D	HOH673
D	HOH676
D	HOH679
D	HOH695
D	HOH697

---

Functional Information from PROSITE/UniProt

site_id	PS00059
Number of Residues	15
Details	ADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEmFGFldgiAqpA

Chain	Residue	Details
A	GLY160-ALA174

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000269|PubMed:23235158

Chain	Residue	Details
A	ASP168
B	ASP168
C	ASP168
D	ASP168

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: axial binding residue => ECO:0000269|PubMed:23235158, ECO:0000269|PubMed:25495127, ECO:0000269|PubMed:25542606, ECO:0000269|DOI:10.1039/c6cy00539j, ECO:0000269|Ref.8, ECO:0007744|PDB:4AU9, ECO:0007744|PDB:4UZI, ECO:0007744|PDB:4W7J, ECO:0007744|PDB:4W7K, ECO:0007744|PDB:4W7L, ECO:0007744|PDB:4W7M, ECO:0007744|PDB:4W7N, ECO:0007744|PDB:4W7O, ECO:0007744|PDB:5AG0, ECO:0007744|PDB:5IKD, ECO:0007744|PDB:5IKG

Chain	Residue	Details
A	HIS304
B	HIS304
C	HIS304
D	HIS304

---

site_id	SWS_FT_FI3
Number of Residues	12
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:23235158, ECO:0000269|PubMed:25542606, ECO:0000269|Ref.8, ECO:0007744|PDB:4AU9, ECO:0007744|PDB:4UZI, ECO:0007744|PDB:5AG0, ECO:0007744|PDB:5AG1

Chain	Residue	Details
A	ASN282
A	ASN349
A	ASN415
B	ASN282
B	ASN349
B	ASN415
C	ASN282
C	ASN349
C	ASN415
D	ASN282
D	ASN349
D	ASN415

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498

Chain	Residue	Details
A	ASN322
B	ASN322
C	ASN322
D	ASN322

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