Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1QPL

FK506 BINDING PROTEIN (12 KDA, HUMAN) COMPLEX WITH L-707,587

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
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

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	BINDING SITE FOR RESIDUE 587 A 108

Chain	Residue
A	TYR26
A	ALA81
A	TYR82
A	ILE91
A	PHE99
C	ILE207
C	SER208
C	GLN253
C	HIS287
C	587308
A	PHE36
A	ASP37
A	ARG42
A	PHE46
A	GLU54
A	VAL55
A	ILE56
A	TRP59

site_id	AC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE 587 C 308

Chain	Residue
A	GLN53
A	GLU54
A	VAL55
A	587108
C	THR206
C	TYR226
C	ASP237
C	PHE246
C	GLU254
C	VAL255
C	ILE256
C	TRP259
C	ALA281
C	TYR282

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	GLN53
C	GLN253

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

Chain	Residue	Details
C	ASP237
C	TYR282
C	ILE256

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	THR227	electrostatic destabiliser, steric role
C	ASP237	electrostatic destabiliser, polar/non-polar interaction, steric role
C	SER238	electrostatic stabiliser, steric role
C	ARG257	electrostatic stabiliser, steric role
C	GLY283	electrostatic stabiliser, steric role
C	ASP300	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)