2N18

Dominant form of the low-affinity complex of yeast cytochrome c and 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
B	0005515	molecular_function	protein binding
B	0005739	cellular_component	mitochondrion
B	0005758	cellular_component	mitochondrial intermembrane space
B	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
B	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
B	0009055	molecular_function	electron transfer activity
B	0020037	molecular_function	heme binding
B	0046872	molecular_function	metal ion binding
B	1901612	molecular_function	cardiolipin binding
C	0005515	molecular_function	protein binding
C	0005739	cellular_component	mitochondrion
C	0005758	cellular_component	mitochondrial intermembrane space
C	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
C	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
C	0009055	molecular_function	electron transfer activity
C	0020037	molecular_function	heme binding
C	0046872	molecular_function	metal ion binding
C	1901612	molecular_function	cardiolipin binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	19
Details	BINDING SITE FOR RESIDUE HEM A 301

Chain	Residue
A	PRO44
A	LEU177
A	GLY178
A	LYS179
A	THR180
A	HIS181
A	ASN184
A	SER185
A	TRP191
A	LEU232
A	THR234
A	VAL45
A	ARG48
A	TRP51
A	PRO145
A	ALA147
A	LEU171
A	ALA174
A	HIS175

---

site_id	AC2
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEC B 201

Chain	Residue
A	ALA193
B	ARG13
B	CYS14
B	CYS17
B	HIS18
B	VAL28
B	PRO30
B	ILE35
B	SER40
B	GLY41
B	TYR46
B	TYR48
B	THR49
B	ASN52
B	TRP59
B	MET64
B	TYR67
B	THR78
B	LYS79
B	MET80
B	CYS81
B	PHE82

---

site_id	AC3
Number of Residues	20
Details	BINDING SITE FOR RESIDUE HEC C 201

Chain	Residue
C	ARG13
C	CYS14
C	CYS17
C	HIS18
C	VAL28
C	SER40
C	GLY41
C	TYR46
C	TYR48
C	THR49
C	ASN52
C	TRP59
C	MET64
C	TYR67
C	THR78
C	LYS79
C	MET80
C	ALA81
C	PHE82
C	LEU94

---

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	2
Details	BINDING: covalent => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5

Chain	Residue	Details
C	CYS14
C	CYS17

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: axial binding residue => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5

Chain	Residue	Details
C	HIS18
C	MET80

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: N6,N6,N6-trimethyllysine; by CTM1 => ECO:0000269|PubMed:10791961, ECO:0000269|PubMed:11880631, ECO:0007744|PDB:1KYO

Chain	Residue	Details
C	LYS72

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: N6,N6,N6-trimethyllysine => ECO:0000269|PubMed:10821864, ECO:0000269|PubMed:18390544

Chain	Residue	Details
C	LYS73

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18407956

Chain	Residue	Details
A	TYR153

---

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

---