Structure of PDB 1bl4 Chain A

Receptor sequence
>1bl4A (length=107) Species: 9606 (Homo sapiens) [Search protein sequence]
GVQVETISPGDGRTFPKRGQTCVVHYTGMLEDGKKVDSSRDRNKPFKFML
GKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGATGHPGIIPPHATLVFD
VELLKLE
3D structure
PDB1bl4 Redesigning an FKBP-ligand interface to generate chemical dimerizers with novel specificity.
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) Y26 V36 D37 I56 Y82 F99
Catalytic site (residue number reindexed from 1) Y26 V36 D37 I56 Y82 F99
Enzyme Commision number 5.2.1.8: peptidylprolyl isomerase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 AP1 A Y26 V36 F46 Q53 E54 V55 I56 W59 Y82 H87 F99 Y26 V36 F46 Q53 E54 V55 I56 W59 Y82 H87 F99 MOAD: ic50=1.8nM
PDBbind-CN: -logKd/Ki=8.74,IC50=1.8nM
BindingDB: IC50=8.2nM
Gene Ontology
Molecular Function
GO:0003755 peptidyl-prolyl cis-trans isomerase activity
GO:0005160 transforming growth factor beta receptor binding
GO:0005515 protein binding
GO:0005527 macrolide binding
GO:0005528 FK506 binding
GO:0016247 channel regulator activity
GO:0030547 signaling receptor inhibitor activity
GO:0034713 type I transforming growth factor beta receptor binding
GO:0044325 transmembrane transporter binding
GO:0070411 I-SMAD binding
GO:0070697 activin receptor binding
Biological Process
GO:0000413 protein peptidyl-prolyl isomerization
GO:0003007 heart morphogenesis
GO:0006457 protein folding
GO:0006458 'de novo' protein folding
GO:0014809 regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion
GO:0022417 protein maturation by protein folding
GO:0030512 negative regulation of transforming growth factor beta receptor signaling pathway
GO:0032092 positive regulation of protein binding
GO:0032880 regulation of protein localization
GO:0032926 negative regulation of activin receptor signaling pathway
GO:0042026 protein refolding
GO:0042110 T cell activation
GO:0043123 positive regulation of canonical NF-kappaB signal transduction
GO:0050776 regulation of immune response
GO:0055010 ventricular cardiac muscle tissue morphogenesis
GO:0060314 regulation of ryanodine-sensitive calcium-release channel activity
GO:0060347 heart trabecula formation
GO:0070588 calcium ion transmembrane transport
GO:0097435 supramolecular fiber organization
GO:1902991 regulation of amyloid precursor protein catabolic process
GO:1990000 amyloid fibril formation
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0014802 terminal cisterna
GO:0016020 membrane
GO:0016529 sarcoplasmic reticulum
GO:0030018 Z disc
GO:0033017 sarcoplasmic reticulum membrane
GO:0098562 cytoplasmic side of membrane
GO:1990425 ryanodine receptor complex

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1bl4, PDBe:1bl4, PDBj:1bl4
PDBsum1bl4
PubMed9724721
UniProtP62942|FKB1A_HUMAN Peptidyl-prolyl cis-trans isomerase FKBP1A (Gene Name=FKBP1A)

[Back to BioLiP]