Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3MDY

Crystal structure of the cytoplasmic domain of the bone morphogenetic protein receptor type-1B (BMPR1B) in complex with FKBP12 and LDN-193189

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0004675	molecular_function	transmembrane receptor protein serine/threonine kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation
A	0007178	biological_process	cell surface receptor protein serine/threonine kinase signaling pathway
A	0016020	cellular_component	membrane
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	0005246	molecular_function	calcium channel regulator activity
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	0010881	biological_process	regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
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	0016529	cellular_component	sarcoplasmic reticulum
B	0016853	molecular_function	isomerase activity
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	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	0051604	biological_process	protein maturation
B	0055010	biological_process	ventricular cardiac muscle tissue morphogenesis
B	0060347	biological_process	heart trabecula formation
B	0070411	molecular_function	I-SMAD binding
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
C	0004672	molecular_function	protein kinase activity
C	0004675	molecular_function	transmembrane receptor protein serine/threonine kinase activity
C	0005524	molecular_function	ATP binding
C	0006468	biological_process	protein phosphorylation
C	0007178	biological_process	cell surface receptor protein serine/threonine kinase signaling pathway
C	0016020	cellular_component	membrane
D	0003007	biological_process	heart morphogenesis
D	0003755	molecular_function	peptidyl-prolyl cis-trans isomerase activity
D	0005160	molecular_function	transforming growth factor beta receptor binding
D	0005246	molecular_function	calcium channel regulator activity
D	0005515	molecular_function	protein binding
D	0005527	molecular_function	macrolide binding
D	0005528	molecular_function	FK506 binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006457	biological_process	protein folding
D	0006458	biological_process	'de novo' protein folding
D	0010881	biological_process	regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
D	0014802	cellular_component	terminal cisterna
D	0014809	biological_process	regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion
D	0016020	cellular_component	membrane
D	0016529	cellular_component	sarcoplasmic reticulum
D	0016853	molecular_function	isomerase activity
D	0030018	cellular_component	Z disc
D	0030512	biological_process	negative regulation of transforming growth factor beta receptor signaling pathway
D	0030547	molecular_function	signaling receptor inhibitor activity
D	0032880	biological_process	regulation of protein localization
D	0032926	biological_process	negative regulation of activin receptor signaling pathway
D	0033017	cellular_component	sarcoplasmic reticulum membrane
D	0034713	molecular_function	type I transforming growth factor beta receptor binding
D	0042026	biological_process	protein refolding
D	0042110	biological_process	T cell activation
D	0043123	biological_process	positive regulation of canonical NF-kappaB signal transduction
D	0044325	molecular_function	transmembrane transporter binding
D	0050776	biological_process	regulation of immune response
D	0051604	biological_process	protein maturation
D	0055010	biological_process	ventricular cardiac muscle tissue morphogenesis
D	0060347	biological_process	heart trabecula formation
D	0070411	molecular_function	I-SMAD binding
D	0070697	molecular_function	activin receptor binding
D	0097435	biological_process	supramolecular fiber organization
D	0098562	cellular_component	cytoplasmic side of membrane
D	1902991	biological_process	regulation of amyloid precursor protein catabolic process
D	1990000	biological_process	amyloid fibril formation
D	1990425	cellular_component	ryanodine receptor complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE LDN A 1

Chain	Residue
A	HOH65
A	ASP289
A	LYS336
A	ASN337
A	LEU339
A	ASP350
A	HOH527
A	HOH715
A	ILE210
A	ALA229
A	LEU259
A	THR279
A	ASP280
A	HIS282
A	GLU283
A	GLY285

site_id	AC2
Number of Residues	17
Details	BINDING SITE FOR RESIDUE LDN C 1

Chain	Residue
C	HOH76
C	HOH93
C	ILE210
C	ALA229
C	LEU259
C	THR279
C	ASP280
C	HIS282
C	GLU283
C	GLY285
C	ASP289
C	LYS336
C	ASN337
C	LEU339
C	ASP350
C	HOH613
C	HOH681

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE210-LYS231

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

Chain	Residue	Details
A	ILE328-VAL340

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	58
Details	Domain: {"description":"GS","evidences":[{"source":"PROSITE-ProRule","id":"PRU00585","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	176
Details	Domain: {"description":"PPIase FKBP-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00277","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P26883","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	6
Details	M-CSA 362

Chain	Residue	Details
C	PRO193	electrostatic destabiliser, steric role
C	GLN203	electrostatic destabiliser, polar/non-polar interaction, steric role
C	ILE204	electrostatic stabiliser, steric role
C	TRP223	electrostatic stabiliser, steric role
C	GLN249	electrostatic stabiliser, steric role
C	ILE266	electrostatic destabiliser, polar/non-polar interaction, steric role

site_id	MCSA2
Number of Residues	6
Details	M-CSA 362

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