Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6OQA

Crystal structure of CEP250 bound to FKBP12 in the presence of FK506-like novel natural product

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000413	biological_process	protein peptidyl-prolyl isomerization
A	0003007	biological_process	heart morphogenesis
A	0003755	molecular_function	peptidyl-prolyl cis-trans isomerase activity
A	0005160	molecular_function	transforming growth factor beta receptor binding
A	0005515	molecular_function	protein binding
A	0005527	molecular_function	macrolide binding
A	0005528	molecular_function	FK506 binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006457	biological_process	protein folding
A	0006458	biological_process	'de novo' protein folding
A	0014802	cellular_component	terminal cisterna
A	0014809	biological_process	regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion
A	0016020	cellular_component	membrane
A	0016247	molecular_function	channel regulator activity
A	0016529	cellular_component	sarcoplasmic reticulum
A	0022417	biological_process	protein maturation by protein folding
A	0030018	cellular_component	Z disc
A	0030512	biological_process	negative regulation of transforming growth factor beta receptor signaling pathway
A	0030547	molecular_function	signaling receptor inhibitor activity
A	0032092	biological_process	positive regulation of protein binding
A	0032880	biological_process	regulation of protein localization
A	0032926	biological_process	negative regulation of activin receptor signaling pathway
A	0033017	cellular_component	sarcoplasmic reticulum membrane
A	0034713	molecular_function	type I transforming growth factor beta receptor binding
A	0042026	biological_process	protein refolding
A	0042110	biological_process	T cell activation
A	0043123	biological_process	positive regulation of canonical NF-kappaB signal transduction
A	0044325	molecular_function	transmembrane transporter binding
A	0050776	biological_process	regulation of immune response
A	0055010	biological_process	ventricular cardiac muscle tissue morphogenesis
A	0060314	biological_process	regulation of ryanodine-sensitive calcium-release channel activity
A	0060347	biological_process	heart trabecula formation
A	0070411	molecular_function	I-SMAD binding
A	0070588	biological_process	calcium ion transmembrane transport
A	0070697	molecular_function	activin receptor binding
A	0097435	biological_process	supramolecular fiber organization
A	0098562	cellular_component	cytoplasmic side of membrane
A	1902991	biological_process	regulation of amyloid precursor protein catabolic process
A	1990000	biological_process	amyloid fibril formation
A	1990425	cellular_component	ryanodine receptor complex
B	0000413	biological_process	protein peptidyl-prolyl isomerization
B	0003007	biological_process	heart morphogenesis
B	0003755	molecular_function	peptidyl-prolyl cis-trans isomerase activity
B	0005160	molecular_function	transforming growth factor beta receptor binding
B	0005515	molecular_function	protein binding
B	0005527	molecular_function	macrolide binding
B	0005528	molecular_function	FK506 binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006457	biological_process	protein folding
B	0006458	biological_process	'de novo' protein folding
B	0014802	cellular_component	terminal cisterna
B	0014809	biological_process	regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion
B	0016020	cellular_component	membrane
B	0016247	molecular_function	channel regulator activity
B	0016529	cellular_component	sarcoplasmic reticulum
B	0022417	biological_process	protein maturation by protein folding
B	0030018	cellular_component	Z disc
B	0030512	biological_process	negative regulation of transforming growth factor beta receptor signaling pathway
B	0030547	molecular_function	signaling receptor inhibitor activity
B	0032092	biological_process	positive regulation of protein binding
B	0032880	biological_process	regulation of protein localization
B	0032926	biological_process	negative regulation of activin receptor signaling pathway
B	0033017	cellular_component	sarcoplasmic reticulum membrane
B	0034713	molecular_function	type I transforming growth factor beta receptor binding
B	0042026	biological_process	protein refolding
B	0042110	biological_process	T cell activation
B	0043123	biological_process	positive regulation of canonical NF-kappaB signal transduction
B	0044325	molecular_function	transmembrane transporter binding
B	0050776	biological_process	regulation of immune response
B	0055010	biological_process	ventricular cardiac muscle tissue morphogenesis
B	0060314	biological_process	regulation of ryanodine-sensitive calcium-release channel activity
B	0060347	biological_process	heart trabecula formation
B	0070411	molecular_function	I-SMAD binding
B	0070588	biological_process	calcium ion transmembrane transport
B	0070697	molecular_function	activin receptor binding
B	0097435	biological_process	supramolecular fiber organization
B	0098562	cellular_component	cytoplasmic side of membrane
B	1902991	biological_process	regulation of amyloid precursor protein catabolic process
B	1990000	biological_process	amyloid fibril formation
B	1990425	cellular_component	ryanodine receptor complex
E	0000413	biological_process	protein peptidyl-prolyl isomerization
E	0003007	biological_process	heart morphogenesis
E	0003755	molecular_function	peptidyl-prolyl cis-trans isomerase activity
E	0005160	molecular_function	transforming growth factor beta receptor binding
E	0005515	molecular_function	protein binding
E	0005527	molecular_function	macrolide binding
E	0005528	molecular_function	FK506 binding
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0006457	biological_process	protein folding
E	0006458	biological_process	'de novo' protein folding
E	0014802	cellular_component	terminal cisterna
E	0014809	biological_process	regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion
E	0016020	cellular_component	membrane
E	0016247	molecular_function	channel regulator activity
E	0016529	cellular_component	sarcoplasmic reticulum
E	0022417	biological_process	protein maturation by protein folding
E	0030018	cellular_component	Z disc
E	0030512	biological_process	negative regulation of transforming growth factor beta receptor signaling pathway
E	0030547	molecular_function	signaling receptor inhibitor activity
E	0032092	biological_process	positive regulation of protein binding
E	0032880	biological_process	regulation of protein localization
E	0032926	biological_process	negative regulation of activin receptor signaling pathway
E	0033017	cellular_component	sarcoplasmic reticulum membrane
E	0034713	molecular_function	type I transforming growth factor beta receptor binding
E	0042026	biological_process	protein refolding
E	0042110	biological_process	T cell activation
E	0043123	biological_process	positive regulation of canonical NF-kappaB signal transduction
E	0044325	molecular_function	transmembrane transporter binding
E	0050776	biological_process	regulation of immune response
E	0055010	biological_process	ventricular cardiac muscle tissue morphogenesis
E	0060314	biological_process	regulation of ryanodine-sensitive calcium-release channel activity
E	0060347	biological_process	heart trabecula formation
E	0070411	molecular_function	I-SMAD binding
E	0070588	biological_process	calcium ion transmembrane transport
E	0070697	molecular_function	activin receptor binding
E	0097435	biological_process	supramolecular fiber organization
E	0098562	cellular_component	cytoplasmic side of membrane
E	1902991	biological_process	regulation of amyloid precursor protein catabolic process
E	1990000	biological_process	amyloid fibril formation
E	1990425	cellular_component	ryanodine receptor complex
F	0000413	biological_process	protein peptidyl-prolyl isomerization
F	0003007	biological_process	heart morphogenesis
F	0003755	molecular_function	peptidyl-prolyl cis-trans isomerase activity
F	0005160	molecular_function	transforming growth factor beta receptor binding
F	0005515	molecular_function	protein binding
F	0005527	molecular_function	macrolide binding
F	0005528	molecular_function	FK506 binding
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0006457	biological_process	protein folding
F	0006458	biological_process	'de novo' protein folding
F	0014802	cellular_component	terminal cisterna
F	0014809	biological_process	regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion
F	0016020	cellular_component	membrane
F	0016247	molecular_function	channel regulator activity
F	0016529	cellular_component	sarcoplasmic reticulum
F	0022417	biological_process	protein maturation by protein folding
F	0030018	cellular_component	Z disc
F	0030512	biological_process	negative regulation of transforming growth factor beta receptor signaling pathway
F	0030547	molecular_function	signaling receptor inhibitor activity
F	0032092	biological_process	positive regulation of protein binding
F	0032880	biological_process	regulation of protein localization
F	0032926	biological_process	negative regulation of activin receptor signaling pathway
F	0033017	cellular_component	sarcoplasmic reticulum membrane
F	0034713	molecular_function	type I transforming growth factor beta receptor binding
F	0042026	biological_process	protein refolding
F	0042110	biological_process	T cell activation
F	0043123	biological_process	positive regulation of canonical NF-kappaB signal transduction
F	0044325	molecular_function	transmembrane transporter binding
F	0050776	biological_process	regulation of immune response
F	0055010	biological_process	ventricular cardiac muscle tissue morphogenesis
F	0060314	biological_process	regulation of ryanodine-sensitive calcium-release channel activity
F	0060347	biological_process	heart trabecula formation
F	0070411	molecular_function	I-SMAD binding
F	0070588	biological_process	calcium ion transmembrane transport
F	0070697	molecular_function	activin receptor binding
F	0097435	biological_process	supramolecular fiber organization
F	0098562	cellular_component	cytoplasmic side of membrane
F	1902991	biological_process	regulation of amyloid precursor protein catabolic process
F	1990000	biological_process	amyloid fibril formation
F	1990425	cellular_component	ryanodine receptor complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	binding site for residue 60Z A 201

Chain	Residue
A	TYR27
A	HIS88
A	PHE100
C	PHE2196
C	PG42303
D	GLN2191
D	ALA2194
D	MET2195
D	GLN2198
A	PHE37
A	ASP38
A	GLN54
A	GLU55
A	VAL56
A	ILE57
A	TRP60
A	TYR83

site_id	AC2
Number of Residues	3
Details	binding site for residue EDO A 202

Chain	Residue
A	ASP80
A	ALA82
A	TYR83

site_id	AC3
Number of Residues	1
Details	binding site for residue EDO A 203

Chain	Residue
A	GLU108

site_id	AC4
Number of Residues	3
Details	binding site for residue EDO A 204

Chain	Residue
A	MET1
A	THR76
A	HOH330

site_id	AC5
Number of Residues	3
Details	binding site for residue PEG A 205

Chain	Residue
A	GLU32
A	LYS74
A	THR76

site_id	AC6
Number of Residues	5
Details	binding site for residue PE8 A 206

Chain	Residue
A	ASN44
A	LYS45
A	LYS48
A	GLU108
A	HOH305

site_id	AC7
Number of Residues	17
Details	binding site for residue 60Z B 201

Chain	Residue
B	TYR27
B	PHE37
B	ASP38
B	GLN54
B	GLU55
B	VAL56
B	ILE57
B	TRP60
B	TYR83
B	HIS88
B	PHE100
B	PE8212
C	GLN2191
C	ALA2194
C	MET2195
C	GLN2198
D	PHE2196

site_id	AC8
Number of Residues	2
Details	binding site for residue EDO B 202

Chain	Residue
B	ARG41
B	ASN44

site_id	AC9
Number of Residues	1
Details	binding site for residue EDO B 203

Chain	Residue
B	LYS106

site_id	AD1
Number of Residues	2
Details	binding site for residue EDO B 205

Chain	Residue
B	LYS53
D	ARG2204

site_id	AD2
Number of Residues	4
Details	binding site for residue EDO B 206

Chain	Residue
B	SER78
B	PRO79
B	ASP80
B	HOH351

site_id	AD3
Number of Residues	1
Details	binding site for residue EDO B 207

Chain	Residue
B	THR7

site_id	AD4
Number of Residues	1
Details	binding site for residue EDO B 208

Chain	Residue
B	LYS74

site_id	AD5
Number of Residues	4
Details	binding site for residue PEG B 209

Chain	Residue
B	GLY2
B	VAL3
B	GLN4
B	THR76

site_id	AD6
Number of Residues	4
Details	binding site for residue PEG B 210

Chain	Residue
B	THR86
B	PRO89
B	HOH342
B	HOH344

site_id	AD7
Number of Residues	3
Details	binding site for residue PEG B 211

Chain	Residue
B	MET30
B	GLU32
B	LYS74

site_id	AD8
Number of Residues	10
Details	binding site for residue PE8 B 212

Chain	Residue
B	ASP80
B	ALA82
B	GLY84
B	THR86
B	60Z201
B	HOH302
B	HOH303
B	HOH345
D	GLU2192
D	PHE2196

site_id	AD9
Number of Residues	2
Details	binding site for residue EDO C 2301

Chain	Residue
C	ASP2175
C	GLN2182

site_id	AE1
Number of Residues	2
Details	binding site for residue PEG C 2302

Chain	Residue
C	PHE2196
C	HOH2414

site_id	AE2
Number of Residues	8
Details	binding site for residue PG4 C 2303

Chain	Residue
A	THR86
A	HIS88
A	60Z201
A	HOH337
C	GLU2192
C	PHE2196
C	HOH2405
C	HOH2407

site_id	AE3
Number of Residues	5
Details	binding site for residue PG4 C 2304

Chain	Residue
B	LYS36
B	PHE37
C	GLN2191
C	HOH2401
D	SER2186

site_id	AE4
Number of Residues	3
Details	binding site for residue PG4 C 2305

Chain	Residue
C	ALA2164
C	GLU2168
C	ARG2160

site_id	AE5
Number of Residues	4
Details	binding site for residue PGE C 2306

Chain	Residue
C	ALA2199
C	SER2200
C	GLU2203
C	HOH2410

site_id	AE6
Number of Residues	6
Details	binding site for residue MG D 2301

Chain	Residue
A	LYS53
D	GLN2209
D	GLN2212
D	PGE2306
D	HOH2413
H	HOH2401

site_id	AE7
Number of Residues	3
Details	binding site for residue EDO D 2302

Chain	Residue
B	GLY90
B	PRO93
D	GLN2182

site_id	AE8
Number of Residues	4
Details	binding site for residue EDO D 2303

Chain	Residue
D	GLN2212
G	GLU2151
G	EDO2301
H	GLN2156

site_id	AE9
Number of Residues	4
Details	binding site for residue PEG D 2304

Chain	Residue
C	ALA2177
D	TRP2169
D	LYS2172
D	HOH2402

site_id	AF1
Number of Residues	1
Details	binding site for residue PEG D 2305

Chain	Residue
D	TRP2169

site_id	AF2
Number of Residues	7
Details	binding site for residue PGE D 2306

Chain	Residue
A	ARG19
A	LYS53
D	GLN2208
D	GLN2209
D	GLN2212
D	MG2301
H	MLA2301

site_id	AF3
Number of Residues	18
Details	binding site for residue 60Z E 201

Chain	Residue
E	TYR27
E	PHE37
E	ASP38
E	GLN54
E	GLU55
E	VAL56
E	ILE57
E	TRP60
E	TYR83
E	HIS88
E	ILE92
E	PHE100
G	PHE2196
G	PGE2304
H	GLN2191
H	ALA2194
H	MET2195
H	GLN2198

site_id	AF4
Number of Residues	1
Details	binding site for residue EDO E 202

Chain	Residue
E	GLN54

site_id	AF5
Number of Residues	1
Details	binding site for residue EDO E 203

Chain	Residue
E	ASP80

site_id	AF6
Number of Residues	17
Details	binding site for residue 60Z F 201

Chain	Residue
F	TYR27
F	PHE37
F	ASP38
F	PHE47
F	GLU55
F	VAL56
F	ILE57
F	TRP60
F	TYR83
F	HIS88
F	ILE92
F	PHE100
G	GLN2191
G	ALA2194
G	MET2195
G	GLN2198
H	PHE2196

site_id	AF7
Number of Residues	1
Details	binding site for residue PEG F 202

Chain	Residue
F	LYS45

site_id	AF8
Number of Residues	3
Details	binding site for residue EDO G 2301

Chain	Residue
D	EDO2303
G	GLU2151
H	GLN2156

site_id	AF9
Number of Residues	3
Details	binding site for residue PEG G 2302

Chain	Residue
A	ARG58
A	TYR81
G	HOH2401

site_id	AG1
Number of Residues	3
Details	binding site for residue PG4 G 2303

Chain	Residue
G	GLU2163
G	GLU2166
H	ARG2165

site_id	AG2
Number of Residues	3
Details	binding site for residue PGE G 2304

Chain	Residue
E	60Z201
G	GLU2192
G	PHE2196

site_id	AG3
Number of Residues	6
Details	binding site for residue MLA H 2301

Chain	Residue
A	ARG19
D	PGE2306
G	ARG2154
H	GLN2156
H	ARG2160
H	HOH2401

site_id	AG4
Number of Residues	2
Details	binding site for residue PEG H 2302

Chain	Residue
H	GLU2168
H	TRP2169

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
C	ALA2194
D	ALA2194
G	ALA2194
H	ALA2194

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	6
Details	M-CSA 362

Chain	Residue	Details
A	TYR27	electrostatic destabiliser, steric role
A	PHE37	electrostatic destabiliser, polar/non-polar interaction, steric role
A	ASP38	electrostatic stabiliser, steric role
A	ILE57	electrostatic stabiliser, steric role
A	TYR83	electrostatic stabiliser, steric role
A	PHE100	electrostatic destabiliser, polar/non-polar interaction, steric role

site_id	MCSA2
Number of Residues	6
Details	M-CSA 362

Chain	Residue	Details
B	TYR27	electrostatic destabiliser, steric role
B	PHE37	electrostatic destabiliser, polar/non-polar interaction, steric role
B	ASP38	electrostatic stabiliser, steric role
B	ILE57	electrostatic stabiliser, steric role
B	TYR83	electrostatic stabiliser, steric role
B	PHE100	electrostatic destabiliser, polar/non-polar interaction, steric role

site_id	MCSA3
Number of Residues	6
Details	M-CSA 362

Chain	Residue	Details
E	TYR27	electrostatic destabiliser, steric role
E	PHE37	electrostatic destabiliser, polar/non-polar interaction, steric role
E	ASP38	electrostatic stabiliser, steric role
E	ILE57	electrostatic stabiliser, steric role
E	TYR83	electrostatic stabiliser, steric role
E	PHE100	electrostatic destabiliser, polar/non-polar interaction, steric role

site_id	MCSA4
Number of Residues	6
Details	M-CSA 362

Chain	Residue	Details
F	TYR27	electrostatic destabiliser, steric role
F	PHE37	electrostatic destabiliser, polar/non-polar interaction, steric role
F	ASP38	electrostatic stabiliser, steric role
F	ILE57	electrostatic stabiliser, steric role
F	TYR83	electrostatic stabiliser, steric role
F	PHE100	electrostatic destabiliser, polar/non-polar interaction, steric role

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