Structure of PDB 1f8a Chain B Binding Site BS01
Receptor Information
>1f8a Chain B (length=155) Species:
9606
(Homo sapiens) [
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GSHGMADEEKLPPGWEKRMSRSSGRVYYFNHITNASQWERPSEPARVRCS
HLLVKHSQSRRPSSWRQEKITRTKEEALELINGYIQKIKSGEEDFESLAS
QFSDCSSAKARGDLGAFSRGQMQKPFEDASFALRTGEMSGPVFTDSGIHI
ILRTE
Ligand information
>1f8a Chain C (length=7) [
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YSPTSPS
Receptor-Ligand Complex Structure
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PDB
1f8a
Structural basis for phosphoserine-proline recognition by group IV WW domains.
Resolution
1.84 Å
Binding residue
(original residue number in PDB)
R18 S20 R21 S22 Y27 F29 N34 S36 Q37 W38 K101 P153
Binding residue
(residue number reindexed from 1)
R18 S20 R21 S22 Y27 F29 N34 S36 Q37 W38 K89 P141
Enzymatic activity
Catalytic site (original residue number in PDB)
Q135 S158
Catalytic site (residue number reindexed from 1)
Q123 S146
Enzyme Commision number
5.2.1.8
: peptidylprolyl isomerase.
Gene Ontology
Molecular Function
GO:0003755
peptidyl-prolyl cis-trans isomerase activity
GO:0003774
cytoskeletal motor activity
GO:0005515
protein binding
GO:0008013
beta-catenin binding
GO:0016859
cis-trans isomerase activity
GO:0031434
mitogen-activated protein kinase kinase binding
GO:0032794
GTPase activating protein binding
GO:0048156
tau protein binding
GO:0050815
phosphoserine residue binding
GO:0050816
phosphothreonine residue binding
GO:0051219
phosphoprotein binding
GO:1990757
ubiquitin ligase activator activity
Biological Process
GO:0000413
protein peptidyl-prolyl isomerization
GO:0001666
response to hypoxia
GO:0001932
regulation of protein phosphorylation
GO:0001934
positive regulation of protein phosphorylation
GO:0007088
regulation of mitotic nuclear division
GO:0010468
regulation of gene expression
GO:0030182
neuron differentiation
GO:0030512
negative regulation of transforming growth factor beta receptor signaling pathway
GO:0031647
regulation of protein stability
GO:0032091
negative regulation of protein binding
GO:0032092
positive regulation of protein binding
GO:0032465
regulation of cytokinesis
GO:0042177
negative regulation of protein catabolic process
GO:0043547
positive regulation of GTPase activity
GO:0045944
positive regulation of transcription by RNA polymerase II
GO:0046785
microtubule polymerization
GO:0050808
synapse organization
GO:0050821
protein stabilization
GO:0060255
regulation of macromolecule metabolic process
GO:0060392
negative regulation of SMAD protein signal transduction
GO:0070373
negative regulation of ERK1 and ERK2 cascade
GO:0080090
regulation of primary metabolic process
GO:0090263
positive regulation of canonical Wnt signaling pathway
GO:1900180
regulation of protein localization to nucleus
GO:1902430
negative regulation of amyloid-beta formation
GO:2000146
negative regulation of cell motility
Cellular Component
GO:0005634
nucleus
GO:0005654
nucleoplasm
GO:0005737
cytoplasm
GO:0005829
cytosol
GO:0016607
nuclear speck
GO:0030496
midbody
GO:0036064
ciliary basal body
GO:0098978
glutamatergic synapse
GO:0099524
postsynaptic cytosol
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:1f8a
,
PDBe:1f8a
,
PDBj:1f8a
PDBsum
1f8a
PubMed
10932246
UniProt
Q13526
|PIN1_HUMAN Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Gene Name=PIN1)
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