2PCC

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	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	0070469	cellular_component	respirasome
B	1901612	molecular_function	cardiolipin binding
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
D	0005515	molecular_function	protein binding
D	0005739	cellular_component	mitochondrion
D	0005758	cellular_component	mitochondrial intermembrane space
D	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
D	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
D	0009055	molecular_function	electron transfer activity
D	0020037	molecular_function	heme binding
D	0046872	molecular_function	metal ion binding
D	0070469	cellular_component	respirasome
D	1901612	molecular_function	cardiolipin binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 299

Chain	Residue
A	ARG48
A	TRP51
A	HIS52
A	HEM296
A	HOH430

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C 300

Chain	Residue
C	ARG48
C	TRP51
C	HIS52
C	HEM296

---

site_id	AC3
Number of Residues	25
Details	BINDING SITE FOR RESIDUE HEM A 296

Chain	Residue
A	PRO44
A	VAL47
A	ARG48
A	TRP51
A	PRO145
A	ASP146
A	ALA147
A	MET172
A	ALA174
A	HIS175
A	LEU177
A	GLY178
A	LYS179
A	THR180
A	HIS181
A	ASN184
A	SER185
A	TRP191
A	LEU232
A	THR234
A	PHE266
A	SO4299
A	HOH302
A	HOH327
A	HOH362

---

site_id	AC4
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEM B 104

Chain	Residue
B	ARG13
B	CYS14
B	CYS17
B	HIS18
B	VAL28
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	ALA81
B	PHE82
B	LEU94
B	HOH321
B	HOH415

---

site_id	AC5
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEM C 296

Chain	Residue
C	PRO44
C	ARG48
C	TRP51
C	PRO145
C	ASP146
C	MET172
C	ALA174
C	HIS175
C	LEU177
C	GLY178
C	LYS179
C	THR180
C	HIS181
C	ASN184
C	SER185
C	TRP191
C	LEU232
C	THR234
C	SO4300
C	HOH665
C	HOH666
C	HOH758

---

site_id	AC6
Number of Residues	21
Details	BINDING SITE FOR RESIDUE HEM D 104

Chain	Residue
D	ARG13
D	CYS14
D	CYS17
D	HIS18
D	VAL28
D	GLY29
D	PRO30
D	ILE35
D	GLY41
D	TYR46
D	TYR48
D	THR49
D	ASN52
D	TRP59
D	MET64
D	TYR67
D	THR78
D	LYS79
D	MET80
D	ALA81
D	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. GPvlVRLaWHIS

Chain	Residue	Details
A	GLY43-SER54

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	BINDING: covalent => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5

Chain	Residue	Details
B	LEU15
B	HIS18
D	LEU15
D	HIS18

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: axial binding residue => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5

Chain	Residue	Details
B	THR19
B	ALA81
D	THR19
D	ALA81

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: N6,N6,N6-trimethyllysine; by CTM1 => ECO:0000269|PubMed:10791961, ECO:0000269|PubMed:11880631, ECO:0007744|PDB:1KYO

Chain	Residue	Details
B	LYS73
D	LYS73

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: N6,N6,N6-trimethyllysine => ECO:0000269|PubMed:10821864, ECO:0000269|PubMed:18390544

Chain	Residue	Details
B	TYR74
D	TYR74

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18407956

Chain	Residue	Details
A	TYR153
C	TYR153

---

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

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