4XVA

Crystal structure of wild type cytochrome c peroxidase

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
A	0034599	biological_process	cellular response to oxidative stress
C	0004601	molecular_function	peroxidase activity
C	0006979	biological_process	response to oxidative stress
C	0020037	molecular_function	heme binding
C	0034599	biological_process	cellular response to oxidative stress
E	0004601	molecular_function	peroxidase activity
E	0006979	biological_process	response to oxidative stress
E	0020037	molecular_function	heme binding
E	0034599	biological_process	cellular response to oxidative stress
G	0004601	molecular_function	peroxidase activity
G	0006979	biological_process	response to oxidative stress
G	0020037	molecular_function	heme binding
G	0034599	biological_process	cellular response to oxidative stress

Functional Information from PDB Data

site_id	AC1
Number of Residues	21
Details	binding site for residue HEM A 1201

Chain	Residue
A	PRO44
A	GLY178
A	LYS179
A	THR180
A	HIS181
A	ASN184
A	SER185
A	TRP191
A	LEU232
A	HOH1313
A	HOH1320
A	ARG48
A	HOH1322
A	HOH1343
A	TRP51
A	PRO145
A	ASP146
A	LEU171
A	MET172
A	ALA174
A	HIS175

---

site_id	AC2
Number of Residues	7
Details	binding site for residue BZI A 1202

Chain	Residue
A	PHE89
A	LEU92
A	GLU93
A	HIS96
A	SER104
A	LEU107
A	PHE108

---

site_id	AC3
Number of Residues	18
Details	binding site for residue HEM C 1201

Chain	Residue
C	PRO44
C	ARG48
C	TRP51
C	PRO145
C	ASP146
C	ALA174
C	HIS175
C	GLY178
C	LYS179
C	THR180
C	HIS181
C	ASN184
C	SER185
C	TRP191
C	LEU232
C	HOH1331
C	HOH1335
C	HOH1375

---

site_id	AC4
Number of Residues	6
Details	binding site for residue BZI C 1202

Chain	Residue
C	PHE89
C	LEU92
C	GLU93
C	HIS96
C	SER104
C	PHE108

---

site_id	AC5
Number of Residues	19
Details	binding site for residue HEM E 1201

Chain	Residue
E	PRO44
E	VAL47
E	ARG48
E	TRP51
E	PRO145
E	ASP146
E	LEU171
E	ALA174
E	HIS175
E	GLY178
E	LYS179
E	THR180
E	HIS181
E	ASN184
E	SER185
E	TRP191
E	LEU232
E	HOH1346
E	HOH1372

---

site_id	AC6
Number of Residues	4
Details	binding site for residue BZI E 1202

Chain	Residue
E	PHE89
E	GLU93
E	HIS96
E	SER104

---

site_id	AC7
Number of Residues	16
Details	binding site for residue HEM G 1201

Chain	Residue
G	PRO44
G	ARG48
G	TRP51
G	PRO145
G	LEU171
G	MET172
G	ALA174
G	HIS175
G	LYS179
G	THR180
G	HIS181
G	ASN184
G	SER185
G	TRP191
G	LEU232
G	HOH1309

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	GLU167-LEU177

---

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

Chain	Residue	Details
A	GLY43-SER54

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton acceptor"}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Tryptophan radical intermediate","evidences":[{"source":"PubMed","id":"2851317","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"10722697","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11170452","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2169873","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6092361","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8384877","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8673607","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	Site: {"description":"Transition state stabilizer"}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	3
Details	M-CSA 709

Chain	Residue	Details
A	ARG48	electrostatic stabiliser
A	HIS52	electrostatic stabiliser, proton acceptor, proton donor
A	TRP191	single electron acceptor, single electron donor

---

site_id	MCSA2
Number of Residues	3
Details	M-CSA 709

Chain

Residue

Details

---

site_id	MCSA3
Number of Residues	3
Details	M-CSA 709

Chain	Residue	Details
C	ARG48	electrostatic stabiliser
C	HIS52	electrostatic stabiliser, proton acceptor, proton donor
C	TRP191	single electron acceptor, single electron donor

---

site_id	MCSA4
Number of Residues	3
Details	M-CSA 709

Chain

Residue

Details

---