Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2B11

Crystal structure of the protein-protein complex between F82W 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	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	1901612	molecular_function	cardiolipin binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	19
Details	BINDING SITE FOR RESIDUE ZNH A 1001

Chain	Residue
A	PRO44
A	LYS179
A	THR180
A	HIS181
A	ASN184
A	SER185
A	TRP191
A	PHE266
A	HOH1401
A	HOH1562
A	HOH1716
A	VAL45
A	VAL47
A	TRP51
A	ASP146
A	LEU171
A	ALA174
A	HIS175
A	GLY178

site_id	AC2
Number of Residues	19
Details	BINDING SITE FOR RESIDUE HEC C 1201

Chain	Residue
C	PRO544
C	TRP551
C	PRO645
C	ASP646
C	LEU671
C	MET672
C	ALA674
C	HIS675
C	GLY678
C	LYS679
C	HIS681
C	ASN684
C	SER685
C	TRP691
C	LEU732
C	THR734
C	HOH1402
C	HOH1433
C	HOH1878

site_id	AC3
Number of Residues	25
Details	BINDING SITE FOR RESIDUE ZNH B 1101

Chain	Residue
A	HOH1841
B	ARG313
B	CYS314
B	CYS317
B	HIS318
B	VAL328
B	ILE335
B	SER340
B	GLY341
B	TYR346
B	TYR348
B	THR349
B	ASN352
B	TRP359
B	MET364
B	TYR367
B	LEU368
B	THR378
B	LYS379
B	MET380
B	ALA381
B	TRP382
B	LEU394
B	HOH1840
B	HOH2444

site_id	AC4
Number of Residues	20
Details	BINDING SITE FOR RESIDUE HEC D 1301

Chain	Residue
D	ARG813
D	CYS814
D	CYS817
D	HIS818
D	VAL828
D	ARG838
D	SER840
D	GLY841
D	TYR846
D	TYR848
D	THR849
D	ASN852
D	TRP859
D	MET864
D	THR878
D	LYS879
D	MET880
D	TRP882
D	LEU894
D	HOH1426

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	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	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	ASN582
C	ARG548
C	HIS552

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	ARG548	electrostatic stabiliser
C	HIS552	electrostatic stabiliser, proton acceptor, proton donor
C	TRP691	single electron acceptor, single electron donor

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