Structure of PDB 1j4r Chain B
Receptor sequence
>1j4rB (length=107) Species:
9606
(Homo sapiens) [
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GVQVETISPGDGRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFML
GKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGATGHPGIIPPHATLVFD
VELLKLE
3D structure
PDB
1j4r
2-Aryl-2,2-difluoroacetamide FKBP12 ligands: synthesis and X-ray structural studies.
Chain
B
Resolution
1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB)
Y26 F36 D37 I56 Y82 F99
Catalytic site (residue number reindexed from 1)
Y26 F36 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
001
B
Y26 F36 D37 R42 F46 Q53 V55 I56 W59 Y82 H87
Y26 F36 D37 R42 F46 Q53 V55 I56 W59 Y82 H87
MOAD
: Ki=0.019uM
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:1j4r
,
PDBe:1j4r
,
PDBj:1j4r
PDBsum
1j4r
PubMed
11735566
UniProt
P62942
|FKB1A_HUMAN Peptidyl-prolyl cis-trans isomerase FKBP1A (Gene Name=FKBP1A)
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