2PCB

CRYSTAL STRUCTURE OF A COMPLEX BETWEEN ELECTRON TRANSFER PARTNERS, CYTOCHROME C PEROXIDASE AND CYTOCHROME C

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
B	0005515	molecular_function	protein binding
B	0005739	cellular_component	mitochondrion
B	0005758	cellular_component	mitochondrial intermembrane space
B	0005829	cellular_component	cytosol
B	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
B	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
B	0006915	biological_process	apoptotic process
B	0008289	molecular_function	lipid binding
B	0009055	molecular_function	electron transfer activity
B	0018063	biological_process	cytochrome c-heme linkage
B	0020037	molecular_function	heme binding
B	0042802	molecular_function	identical protein binding
B	0046872	molecular_function	metal ion binding
B	0070069	cellular_component	cytochrome complex
B	0097190	biological_process	apoptotic signaling pathway
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

Functional Information from PDB Data

site_id	AC1
Number of Residues	21
Details	BINDING SITE FOR RESIDUE HEM A 295

Chain	Residue
A	PRO44
A	GLY178
A	LYS179
A	THR180
A	HIS181
A	ASN184
A	SER185
A	TRP191
A	LEU232
A	THR234
A	PHE266
A	ARG48
A	HOH364
A	HOH397
A	TRP51
A	PRO145
A	ASP146
A	MET172
A	ALA174
A	HIS175
A	LEU177

---

site_id	AC2
Number of Residues	18
Details	BINDING SITE FOR RESIDUE HEM B 105

Chain	Residue
B	LYS13
B	CYS14
B	CYS17
B	HIS18
B	THR28
B	LYS39
B	THR40
B	GLY41
B	PHE46
B	TYR48
B	THR49
B	ASN52
B	TRP59
B	TYR67
B	THR78
B	LYS79
B	MET80
B	PHE82

---

site_id	AC3
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEM C 295

Chain	Residue
C	PRO44
C	VAL47
C	ARG48
C	TRP51
C	ASP146
C	PHE158
C	MET172
C	ALA174
C	HIS175
C	LEU177
C	GLY178
C	LYS179
C	THR180
C	HIS181
C	ASN184
C	SER185
C	TRP191
C	THR234
C	HOH603
C	HOH606
C	HOH610
C	HOH616

---

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. GPvlVRLaWHIS

Chain	Residue	Details
A	GLY43-SER54

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton acceptor"}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
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	2
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	2
Details	Site: {"description":"Transition state stabilizer"}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Binding site: {"description":"covalent"}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"5545094","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	Binding site: {"description":"axial binding residue"}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	Modified residue: {"description":"N-acetylglycine","evidences":[{"source":"PubMed","id":"14469771","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P62894","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	1
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P62897","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
Number of Residues	1
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62897","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI13
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P62897","evidenceCode":"ECO:0000250"}]}

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	ARG48
A	HIS52
A	ASN82

---

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1apx

Chain	Residue	Details
C	ARG48
C	HIS52
C	ASN82

---

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

---