Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6M4U

Crystal structure of FKBP-FRB T2098L mutant in complex with rapamycin

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	0044877	molecular_function	protein-containing complex binding
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	0044877	molecular_function	protein-containing complex binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	19
Details	binding site for residue RAP A 201

Chain	Residue
A	TYR27
A	TYR83
A	PHE100
A	HOH309
A	HOH323
B	LEU2031
B	SER2035
B	LEU2098
B	TYR2105
B	PHE2108
F	LYS2113
A	PHE37
A	ASP38
A	PHE47
A	GLN54
A	GLU55
A	VAL56
A	ILE57
A	TRP60

site_id	AC2
Number of Residues	4
Details	binding site for residue ZN A 202

Chain	Residue
A	GLU55
B	ARG2109
F	LYS2113
F	HOH2346

site_id	AC3
Number of Residues	5
Details	binding site for residue ZN A 203

Chain	Residue
A	GLU108
A	CL205
E	LYS48
E	GLU108
E	CL203

site_id	AC4
Number of Residues	5
Details	binding site for residue ZN A 204

Chain	Residue
A	LYS48
A	GLU108
A	CL206
E	GLU108
E	CL204

site_id	AC5
Number of Residues	2
Details	binding site for residue CL A 205

Chain	Residue
A	GLU108
A	ZN203

site_id	AC6
Number of Residues	3
Details	binding site for residue CL A 206

Chain	Residue
A	LYS48
A	LYS106
A	ZN204

site_id	AC7
Number of Residues	4
Details	binding site for residue ZN B 2201

Chain	Residue
B	HIS2028
B	GLU2032
B	CL2207
F	GLU2025

site_id	AC8
Number of Residues	4
Details	binding site for residue ZN B 2202

Chain	Residue
B	ASP2077
B	HIS2106
B	ARG2110
B	HOH2301

site_id	AC9
Number of Residues	5
Details	binding site for residue ZN B 2203

Chain	Residue
B	HIS2024
B	LYS2113
B	HOH2340
B	HOH2347
B	HOH2350

site_id	AD1
Number of Residues	2
Details	binding site for residue ZN B 2204

Chain	Residue
B	GLU2083
B	HOH2328

site_id	AD2
Number of Residues	2
Details	binding site for residue ZN B 2205

Chain	Residue
B	HIS2106
B	HOH2335

site_id	AD3
Number of Residues	7
Details	binding site for residue CL B 2206

Chain	Residue
B	GLU2025
B	HIS2028
B	SER2112
B	LYS2113
F	ZN2201
F	HIS2028
F	GLU2032

site_id	AD4
Number of Residues	7
Details	binding site for residue CL B 2207

Chain	Residue
B	HIS2028
B	GLU2032
B	ZN2201
F	HIS2024
F	GLU2025
F	SER2112
F	LYS2113

site_id	AD5
Number of Residues	4
Details	binding site for residue ZN F 2201

Chain	Residue
B	GLU2025
B	CL2206
F	HIS2028
F	GLU2032

site_id	AD6
Number of Residues	3
Details	binding site for residue ZN F 2202

Chain	Residue
B	GLU2029
B	HOH2339
F	GLY2019

site_id	AD7
Number of Residues	25
Details	binding site for residue RAP E 201

Chain	Residue
F	TYR2105
F	PHE2108
B	LYS2113
E	TYR27
E	PHE37
E	ASP38
E	PHE47
E	GLN54
E	GLU55
E	VAL56
E	ILE57
E	TRP60
E	TYR83
E	ILE92
E	HOH316
E	HOH327
E	HOH331
E	HOH338
E	HOH350
F	LEU2031
F	GLU2032
F	SER2035
F	PHE2039
F	LEU2098
F	ASP2102

site_id	AD8
Number of Residues	2
Details	binding site for residue ZN E 202

Chain	Residue
E	HIS95
E	HOH357

site_id	AD9
Number of Residues	2
Details	binding site for residue CL E 203

Chain	Residue
A	ZN203
E	LYS48

site_id	AE1
Number of Residues	2
Details	binding site for residue CL E 204

Chain	Residue
A	ZN204
E	LEU107

site_id	AE2
Number of Residues	3
Details	binding site for residue GOL F 2203

Chain	Residue
F	GLU2080
F	GLU2083
F	HOH2310

site_id	AE3
Number of Residues	4
Details	binding site for residue ZN F 2204

Chain	Residue
F	HIS2024
F	CL2207
F	HOH2344
F	HOH2352

site_id	AE4
Number of Residues	6
Details	binding site for residue ZN F 2205

Chain	Residue
F	ARG2076
F	ASP2077
F	HIS2106
F	ARG2110
F	HOH2324
F	HOH2327

site_id	AE5
Number of Residues	3
Details	binding site for residue ZN F 2206

Chain	Residue
F	GLU2052
F	GLN2082
F	HOH2363

site_id	AE6
Number of Residues	3
Details	binding site for residue CL F 2207

Chain	Residue
F	TRP2023
F	HIS2024
F	ZN2204

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250\|UniProtKB:P26883

Chain	Residue	Details
A	LYS53
E	LYS53

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
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

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