Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5CIH

Complex of yeast cytochrome c peroxidase (W191Y) with iso-1 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	0022904	biological_process	respiratory electron transport chain
B	0046872	molecular_function	metal ion binding
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	0022904	biological_process	respiratory electron transport chain
D	0046872	molecular_function	metal ion binding
D	1901612	molecular_function	cardiolipin binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	binding site for residue HEC A 301

Chain	Residue
A	PRO44
A	HIS181
A	SER185
A	TYR191
A	ARG48
A	PRO145
A	ALA174
A	HIS175
A	LEU177
A	GLY178
A	LYS179
A	THR180

site_id	AC2
Number of Residues	22
Details	binding site for residue HEC B 201

Chain	Residue
A	ALA193
A	ALA194
B	ARG13
B	CYS14
B	GLN16
B	CYS17
B	HIS18
B	VAL28
B	GLY29
B	PRO30
B	SER40
B	GLY41
B	GLN42
B	TYR46
B	TYR48
B	THR49
B	TYR67
B	LEU68
B	THR78
B	LYS79
B	MET80
B	LEU94

site_id	AC3
Number of Residues	17
Details	binding site for residue HEC C 301

Chain	Residue
C	PRO44
C	VAL47
C	ARG48
C	TRP51
C	PRO145
C	ASP146
C	ALA174
C	HIS175
C	LEU177
C	GLY178
C	LYS179
C	THR180
C	HIS181
C	ASN184
C	SER185
C	TYR191
C	THR234

site_id	AC4
Number of Residues	22
Details	binding site for residue HEC D 201

Chain	Residue
C	ALA193
C	ALA194
D	LEU9
D	PHE10
D	THR12
D	ARG13
D	LEU15
D	GLN16
D	CYS17
D	HIS18
D	VAL28
D	GLY29
D	PRO30
D	GLY41
D	TYR46
D	THR49
D	ASN52
D	TRP59
D	THR78
D	MET80
D	PHE82
D	HOH304

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	4
Details	Binding site: {"description":"covalent","evidences":[{"source":"PubMed","id":"11880631","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KYO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CX5","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	4
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"11880631","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KYO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CX5","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Modified residue: {"description":"N6,N6,N6-trimethyllysine; by CTM1","evidences":[{"source":"PubMed","id":"10791961","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11880631","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KYO","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	2
Details	Modified residue: {"description":"N6,N6,N6-trimethyllysine","evidences":[{"source":"PubMed","id":"10821864","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"}]}

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	TYR191	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	TYR191	single electron acceptor, single electron donor

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)