Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1B6C

CRYSTAL STRUCTURE OF THE CYTOPLASMIC DOMAIN OF THE TYPE I TGF-BETA RECEPTOR IN COMPLEX WITH FKBP12

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	0004672	molecular_function	protein kinase activity
B	0004675	molecular_function	transmembrane receptor protein serine/threonine kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation
B	0007178	biological_process	cell surface receptor protein serine/threonine kinase signaling pathway
B	0016020	cellular_component	membrane
C	0000413	biological_process	protein peptidyl-prolyl isomerization
C	0003007	biological_process	heart morphogenesis
C	0003755	molecular_function	peptidyl-prolyl cis-trans isomerase activity
C	0005160	molecular_function	transforming growth factor beta receptor binding
C	0005515	molecular_function	protein binding
C	0005527	molecular_function	macrolide binding
C	0005528	molecular_function	FK506 binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006457	biological_process	protein folding
C	0006458	biological_process	'de novo' protein folding
C	0014802	cellular_component	terminal cisterna
C	0014809	biological_process	regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion
C	0016020	cellular_component	membrane
C	0016247	molecular_function	channel regulator activity
C	0016529	cellular_component	sarcoplasmic reticulum
C	0022417	biological_process	protein maturation by protein folding
C	0030018	cellular_component	Z disc
C	0030512	biological_process	negative regulation of transforming growth factor beta receptor signaling pathway
C	0030547	molecular_function	signaling receptor inhibitor activity
C	0032092	biological_process	positive regulation of protein binding
C	0032880	biological_process	regulation of protein localization
C	0032926	biological_process	negative regulation of activin receptor signaling pathway
C	0033017	cellular_component	sarcoplasmic reticulum membrane
C	0034713	molecular_function	type I transforming growth factor beta receptor binding
C	0042026	biological_process	protein refolding
C	0042110	biological_process	T cell activation
C	0043123	biological_process	positive regulation of canonical NF-kappaB signal transduction
C	0044325	molecular_function	transmembrane transporter binding
C	0050776	biological_process	regulation of immune response
C	0055010	biological_process	ventricular cardiac muscle tissue morphogenesis
C	0060314	biological_process	regulation of ryanodine-sensitive calcium-release channel activity
C	0060347	biological_process	heart trabecula formation
C	0070411	molecular_function	I-SMAD binding
C	0070588	biological_process	calcium ion transmembrane transport
C	0070697	molecular_function	activin receptor binding
C	0097435	biological_process	supramolecular fiber organization
C	0098562	cellular_component	cytoplasmic side of membrane
C	1902991	biological_process	regulation of amyloid precursor protein catabolic process
C	1990000	biological_process	amyloid fibril formation
C	1990425	cellular_component	ryanodine receptor complex
D	0004672	molecular_function	protein kinase activity
D	0004675	molecular_function	transmembrane receptor protein serine/threonine kinase activity
D	0005524	molecular_function	ATP binding
D	0006468	biological_process	protein phosphorylation
D	0007178	biological_process	cell surface receptor protein serine/threonine kinase signaling pathway
D	0016020	cellular_component	membrane
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	0004672	molecular_function	protein kinase activity
F	0004675	molecular_function	transmembrane receptor protein serine/threonine kinase activity
F	0005524	molecular_function	ATP binding
F	0006468	biological_process	protein phosphorylation
F	0007178	biological_process	cell surface receptor protein serine/threonine kinase signaling pathway
F	0016020	cellular_component	membrane
G	0000413	biological_process	protein peptidyl-prolyl isomerization
G	0003007	biological_process	heart morphogenesis
G	0003755	molecular_function	peptidyl-prolyl cis-trans isomerase activity
G	0005160	molecular_function	transforming growth factor beta receptor binding
G	0005515	molecular_function	protein binding
G	0005527	molecular_function	macrolide binding
G	0005528	molecular_function	FK506 binding
G	0005737	cellular_component	cytoplasm
G	0005829	cellular_component	cytosol
G	0006457	biological_process	protein folding
G	0006458	biological_process	'de novo' protein folding
G	0014802	cellular_component	terminal cisterna
G	0014809	biological_process	regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion
G	0016020	cellular_component	membrane
G	0016247	molecular_function	channel regulator activity
G	0016529	cellular_component	sarcoplasmic reticulum
G	0022417	biological_process	protein maturation by protein folding
G	0030018	cellular_component	Z disc
G	0030512	biological_process	negative regulation of transforming growth factor beta receptor signaling pathway
G	0030547	molecular_function	signaling receptor inhibitor activity
G	0032092	biological_process	positive regulation of protein binding
G	0032880	biological_process	regulation of protein localization
G	0032926	biological_process	negative regulation of activin receptor signaling pathway
G	0033017	cellular_component	sarcoplasmic reticulum membrane
G	0034713	molecular_function	type I transforming growth factor beta receptor binding
G	0042026	biological_process	protein refolding
G	0042110	biological_process	T cell activation
G	0043123	biological_process	positive regulation of canonical NF-kappaB signal transduction
G	0044325	molecular_function	transmembrane transporter binding
G	0050776	biological_process	regulation of immune response
G	0055010	biological_process	ventricular cardiac muscle tissue morphogenesis
G	0060314	biological_process	regulation of ryanodine-sensitive calcium-release channel activity
G	0060347	biological_process	heart trabecula formation
G	0070411	molecular_function	I-SMAD binding
G	0070588	biological_process	calcium ion transmembrane transport
G	0070697	molecular_function	activin receptor binding
G	0097435	biological_process	supramolecular fiber organization
G	0098562	cellular_component	cytoplasmic side of membrane
G	1902991	biological_process	regulation of amyloid precursor protein catabolic process
G	1990000	biological_process	amyloid fibril formation
G	1990425	cellular_component	ryanodine receptor complex
H	0004672	molecular_function	protein kinase activity
H	0004675	molecular_function	transmembrane receptor protein serine/threonine kinase activity
H	0005524	molecular_function	ATP binding
H	0006468	biological_process	protein phosphorylation
H	0007178	biological_process	cell surface receptor protein serine/threonine kinase signaling pathway
H	0016020	cellular_component	membrane

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 158

Chain	Residue
B	ARG377
B	LEU426
B	ASP435

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 D 504

Chain	Residue
D	ARG377
D	LEU426
D	ASP435

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 F 504

Chain	Residue
F	ARG377
F	LEU426
F	ASP435

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 H 504

Chain	Residue
H	ARG377
H	LEU426
H	ASP435

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	22
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGKGRFGEVWrGkwrgee............VAVK

Chain	Residue	Details
B	ILE211-LYS232

site_id	PS00108
Number of Residues	13
Details	PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IaHrDLKskNILV

Chain	Residue	Details
B	ILE329-VAL341

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000255\|PROSITE-ProRule:PRU00159, ECO:0000255\|PROSITE-ProRule:PRU10027

Chain	Residue	Details
B	ASP333
D	ASP333
F	ASP333
H	ASP333

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU00159

Chain	Residue	Details
B	ILE211
B	LYS232
D	ILE211
D	LYS232
F	ILE211
F	LYS232
H	ILE211
H	LYS232

site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:19369195

Chain	Residue	Details
B	SER165
D	SER165
F	SER165
H	SER165

site_id	SWS_FT_FI4
Number of Residues	8
Details	MOD_RES: Phosphothreonine; by TGFBR2 => ECO:0000269\|PubMed:7774578

Chain	Residue	Details
B	THR185
B	THR186
D	THR185
D	THR186
F	THR185
F	THR186
H	THR185
H	THR186

site_id	SWS_FT_FI5
Number of Residues	12
Details	MOD_RES: Phosphoserine; by TGFBR2 => ECO:0000269\|PubMed:7774578

Chain	Residue	Details
B	SER187
H	SER187
H	SER189
H	SER191
B	SER189
B	SER191
D	SER187
D	SER189
D	SER191
F	SER187
F	SER189
F	SER191

site_id	SWS_FT_FI6
Number of Residues	8
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000250

Chain	Residue	Details
B	LYS391
D	LYS391
F	LYS391
H	LYS391

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1d6o

Chain	Residue	Details
A	ILE56
A	TYR82
A	ASP37

site_id	CSA10
Number of Residues	2
Details	Annotated By Reference To The Literature 1d6o

Chain	Residue	Details
D	LYS335
D	ASP333

site_id	CSA11
Number of Residues	2
Details	Annotated By Reference To The Literature 1d6o

Chain	Residue	Details
F	LYS335
F	ASP333

site_id	CSA12
Number of Residues	2
Details	Annotated By Reference To The Literature 1d6o

Chain	Residue	Details
H	LYS335
H	ASP333

site_id	CSA13
Number of Residues	3
Details	Annotated By Reference To The Literature 1d6o

Chain	Residue	Details
B	THR375
B	LYS335
B	ASP333

site_id	CSA14
Number of Residues	3
Details	Annotated By Reference To The Literature 1d6o

Chain	Residue	Details
D	THR375
D	LYS335
D	ASP333

site_id	CSA15
Number of Residues	3
Details	Annotated By Reference To The Literature 1d6o

Chain	Residue	Details
F	THR375
F	LYS335
F	ASP333

site_id	CSA16
Number of Residues	3
Details	Annotated By Reference To The Literature 1d6o

Chain	Residue	Details
H	THR375
H	LYS335
H	ASP333

site_id	CSA17
Number of Residues	3
Details	Annotated By Reference To The Literature 1d6o

Chain	Residue	Details
B	ASN338
B	LYS335
B	ASP333

site_id	CSA18
Number of Residues	3
Details	Annotated By Reference To The Literature 1d6o

Chain	Residue	Details
D	ASN338
D	LYS335
D	ASP333

site_id	CSA19
Number of Residues	3
Details	Annotated By Reference To The Literature 1d6o

Chain	Residue	Details
F	ASN338
F	LYS335
F	ASP333

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1d6o

Chain	Residue	Details
C	ILE56
C	TYR82
C	ASP37

site_id	CSA20
Number of Residues	3
Details	Annotated By Reference To The Literature 1d6o

Chain	Residue	Details
H	ASN338
H	LYS335
H	ASP333

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1d6o

Chain	Residue	Details
E	ILE56
E	TYR82
E	ASP37

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1d6o

Chain	Residue	Details
G	ILE56
G	TYR82
G	ASP37

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1d6o

Chain	Residue	Details
B	LYS337
B	ASP333

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1d6o

Chain	Residue	Details
D	LYS337
D	ASP333

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 1d6o

Chain	Residue	Details
F	LYS337
F	ASP333

site_id	CSA8
Number of Residues	2
Details	Annotated By Reference To The Literature 1d6o

Chain	Residue	Details
H	LYS337
H	ASP333

site_id	CSA9
Number of Residues	2
Details	Annotated By Reference To The Literature 1d6o

Chain	Residue	Details
B	LYS335
B	ASP333

site_id	MCSA1
Number of Residues	6
Details	M-CSA 362

Chain	Residue	Details
A	THR27	electrostatic destabiliser, steric role
A	ASP37	electrostatic destabiliser, polar/non-polar interaction, steric role
A	SER38	electrostatic stabiliser, steric role
A	ARG57	electrostatic stabiliser, steric role
A	GLY83	electrostatic stabiliser, steric role
A	ASP100	electrostatic destabiliser, polar/non-polar interaction, steric role

site_id	MCSA2
Number of Residues	6
Details	M-CSA 362

Chain	Residue	Details
C	THR27	electrostatic destabiliser, steric role
C	ASP37	electrostatic destabiliser, polar/non-polar interaction, steric role
C	SER38	electrostatic stabiliser, steric role
C	ARG57	electrostatic stabiliser, steric role
C	GLY83	electrostatic stabiliser, steric role
C	ASP100	electrostatic destabiliser, polar/non-polar interaction, steric role

site_id	MCSA3
Number of Residues	6
Details	M-CSA 362

Chain	Residue	Details
E	THR27	electrostatic destabiliser, steric role
E	ASP37	electrostatic destabiliser, polar/non-polar interaction, steric role
E	SER38	electrostatic stabiliser, steric role
E	ARG57	electrostatic stabiliser, steric role
E	GLY83	electrostatic stabiliser, steric role
E	ASP100	electrostatic destabiliser, polar/non-polar interaction, steric role

site_id	MCSA4
Number of Residues	6
Details	M-CSA 362

Chain	Residue	Details
G	THR27	electrostatic destabiliser, steric role
G	ASP37	electrostatic destabiliser, polar/non-polar interaction, steric role
G	SER38	electrostatic stabiliser, steric role
G	ARG57	electrostatic stabiliser, steric role
G	GLY83	electrostatic stabiliser, steric role
G	ASP100	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)