Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4RSZ

The X-ray structure of the Primary Adduct formed in the Reaction between Cisplatin and Cytochrome c

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005758	cellular_component	mitochondrial intermembrane space
A	0005829	cellular_component	cytosol
A	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
A	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
A	0006915	biological_process	apoptotic process
A	0008289	molecular_function	lipid binding
A	0009055	molecular_function	electron transfer activity
A	0020037	molecular_function	heme binding
A	0022904	biological_process	respiratory electron transport chain
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding
A	0070069	cellular_component	cytochrome complex
A	0097190	biological_process	apoptotic signaling pathway
B	0005515	molecular_function	protein binding
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	0020037	molecular_function	heme binding
B	0022904	biological_process	respiratory electron transport chain
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	0005515	molecular_function	protein binding
C	0005758	cellular_component	mitochondrial intermembrane space
C	0005829	cellular_component	cytosol
C	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
C	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
C	0006915	biological_process	apoptotic process
C	0008289	molecular_function	lipid binding
C	0009055	molecular_function	electron transfer activity
C	0020037	molecular_function	heme binding
C	0022904	biological_process	respiratory electron transport chain
C	0042802	molecular_function	identical protein binding
C	0046872	molecular_function	metal ion binding
C	0070069	cellular_component	cytochrome complex
C	0097190	biological_process	apoptotic signaling pathway
D	0005515	molecular_function	protein binding
D	0005758	cellular_component	mitochondrial intermembrane space
D	0005829	cellular_component	cytosol
D	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
D	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
D	0006915	biological_process	apoptotic process
D	0008289	molecular_function	lipid binding
D	0009055	molecular_function	electron transfer activity
D	0020037	molecular_function	heme binding
D	0022904	biological_process	respiratory electron transport chain
D	0042802	molecular_function	identical protein binding
D	0046872	molecular_function	metal ion binding
D	0070069	cellular_component	cytochrome complex
D	0097190	biological_process	apoptotic signaling pathway
E	0005515	molecular_function	protein binding
E	0005758	cellular_component	mitochondrial intermembrane space
E	0005829	cellular_component	cytosol
E	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
E	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
E	0006915	biological_process	apoptotic process
E	0008289	molecular_function	lipid binding
E	0009055	molecular_function	electron transfer activity
E	0020037	molecular_function	heme binding
E	0022904	biological_process	respiratory electron transport chain
E	0042802	molecular_function	identical protein binding
E	0046872	molecular_function	metal ion binding
E	0070069	cellular_component	cytochrome complex
E	0097190	biological_process	apoptotic signaling pathway
F	0005515	molecular_function	protein binding
F	0005758	cellular_component	mitochondrial intermembrane space
F	0005829	cellular_component	cytosol
F	0006122	biological_process	mitochondrial electron transport, ubiquinol to cytochrome c
F	0006123	biological_process	mitochondrial electron transport, cytochrome c to oxygen
F	0006915	biological_process	apoptotic process
F	0008289	molecular_function	lipid binding
F	0009055	molecular_function	electron transfer activity
F	0020037	molecular_function	heme binding
F	0022904	biological_process	respiratory electron transport chain
F	0042802	molecular_function	identical protein binding
F	0046872	molecular_function	metal ion binding
F	0070069	cellular_component	cytochrome complex
F	0097190	biological_process	apoptotic signaling pathway

Functional Information from PDB Data

site_id	AC1
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEC A 201

Chain	Residue
A	LYS13
A	TYR48
A	THR49
A	ASN52
A	TRP59
A	TYR67
A	LEU68
A	THR78
A	LYS79
A	MET80
A	ILE81
A	CYS14
A	PHE82
A	LEU94
A	HOH305
A	CYS17
A	HIS18
A	THR28
A	PRO30
A	ARG38
A	THR40
A	GLY41

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CPT A 202

Chain	Residue
A	GLU61
A	MET65
A	GLU92

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE NO3 A 203

Chain	Residue
A	PHE10
A	THR19
A	VAL20
A	GLU21
A	HOH310
C	THR28
C	ILE81
C	HOH302

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NO3 A 204

Chain	Residue
A	PHE82
A	ALA83
A	GLY84
B	LYS8
B	VAL11
B	GLN12

site_id	AC5
Number of Residues	21
Details	BINDING SITE FOR RESIDUE HEC B 201

Chain	Residue
B	LYS13
B	CYS14
B	GLN16
B	CYS17
B	HIS18
B	THR28
B	GLY29
B	PRO30
B	THR40
B	GLY41
B	TYR48
B	THR49
B	ASN52
B	TRP59
B	TYR67
B	LEU68
B	THR78
B	LYS79
B	MET80
B	LEU94
B	HOH307

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 202

Chain	Residue
A	LYS72
B	LYS100
B	GLU104
E	GLY23

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CPT B 203

Chain	Residue
B	GLU61
B	GLU62
B	MET65
B	GLU92
E	GLU62

site_id	AC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE NO3 B 204

Chain	Residue
A	THR28
A	ILE81
B	PHE10
B	THR19
B	VAL20
B	GLU21
B	HOH306
B	HOH318

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NO3 B 205

Chain	Residue
B	PHE82
B	ALA83
B	GLY84
C	LYS8
C	VAL11
C	GLN12

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NO3 B 206

Chain	Residue
B	GLY41
B	PHE46
B	THR47
B	TYR48

site_id	BC2
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEC C 201

Chain	Residue
C	ASN52
C	TRP59
C	TYR67
C	LEU68
C	THR78
C	LYS79
C	MET80
C	ILE81
C	LEU94
C	HOH308
C	LYS13
C	CYS14
C	GLN16
C	CYS17
C	HIS18
C	THR28
C	PRO30
C	ARG38
C	THR40
C	GLY41
C	TYR48
C	THR49

site_id	BC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE NO3 C 202

Chain	Residue
B	THR28
B	ILE81
C	PHE10
C	THR19
C	VAL20
C	GLU21
C	HOH304
C	HOH305

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NO3 C 203

Chain	Residue
A	LYS8
A	VAL11
A	GLN12
C	PHE82
C	ALA83
C	GLY84

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE NO3 C 204

Chain	Residue
B	ALA83
C	GLU4
C	LYS7

site_id	BC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE NO3 C 205

Chain	Residue
C	PHE36
C	LYS99
F	LYS22

site_id	BC7
Number of Residues	21
Details	BINDING SITE FOR RESIDUE HEC D 201

Chain	Residue
D	LYS13
D	CYS14
D	GLN16
D	CYS17
D	HIS18
D	THR28
D	GLY29
D	PRO30
D	ARG38
D	GLY41
D	TYR48
D	THR49
D	ASN52
D	TRP59
D	TYR67
D	LEU68
D	THR78
D	LYS79
D	MET80
D	LEU94
D	HOH301

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CPT D 202

Chain	Residue
A	GLU61
D	GLU61
D	GLU62
D	MET65
D	GLU92

site_id	BC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE NO3 D 203

Chain	Residue
D	PHE10
D	THR19
D	VAL20
D	GLU21
D	HOH310
D	HOH318
F	THR28
F	ILE81

site_id	CC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NO3 D 204

Chain	Residue
D	PHE82
D	ALA83
D	GLY84
E	LYS8
E	VAL11
E	GLN12

site_id	CC2
Number of Residues	20
Details	BINDING SITE FOR RESIDUE HEC E 201

Chain	Residue
E	LYS13
E	CYS14
E	CYS17
E	HIS18
E	THR28
E	GLY29
E	ARG38
E	THR40
E	GLY41
E	TYR48
E	THR49
E	ASN52
E	TRP59
E	TYR67
E	LEU68
E	THR78
E	LYS79
E	MET80
E	LEU94
E	HOH301

site_id	CC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CPT E 202

Chain	Residue
E	MET65

site_id	CC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NO3 E 203

Chain	Residue
E	HIS26
E	PRO30
E	ASN31
E	ALA43
E	PRO44
E	GLY45
E	PHE46

site_id	CC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NO3 E 204

Chain	Residue
E	PHE82
E	ALA83
E	GLY84
F	LYS8
F	VAL11
F	GLN12

site_id	CC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NO3 E 205

Chain	Residue
D	THR28
D	ILE81
E	PHE10
E	THR19
E	VAL20
E	GLU21
E	HOH309

site_id	CC7
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEC F 201

Chain	Residue
F	LYS13
F	CYS14
F	GLN16
F	CYS17
F	HIS18
F	THR28
F	GLY29
F	PRO30
F	ARG38
F	THR40
F	GLY41
F	TYR48
F	THR49
F	ASN52
F	TRP59
F	TYR67
F	THR78
F	LYS79
F	MET80
F	ILE81
F	LEU94
F	HOH311

site_id	CC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SO4 F 202

Chain	Residue
D	LYS25
D	LYS27
E	LYS25
E	LYS27
F	GLN16
F	LYS25
F	LYS27
F	HOH303
F	HOH304
F	HOH308

site_id	CC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CPT F 203

Chain	Residue
F	GLU61
F	MET65
F	GLU92

site_id	DC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NO3 F 204

Chain	Residue
E	THR28
E	ILE81
E	HOH312
F	THR19
F	VAL20
F	GLU21
F	HOH313

site_id	DC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NO3 F 205

Chain	Residue
D	LYS8
D	VAL11
D	GLN12
F	PHE82
F	ALA83
F	GLY84

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	Binding site: {"description":"covalent"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	6
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_FI3
Number of Residues	6
Details	Binding site: {"description":"axial binding residue"}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	6
Details	Modified residue: {"description":"N-acetylglycine","evidences":[{"source":"PubMed","id":"14469771","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	12
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P62894","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	6
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P62897","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	6
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62897","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	6
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P62897","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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