Structure of PDB 7f0m Chain C
Receptor sequence
>7f0mC (length=146) Species:
9606
(Homo sapiens) [
Search protein sequence
]
KLPPGWEKAMSRSSGRVYYFNHITNASQWERPSEPARVRCSHLLVKHSQS
RRPSSWRQEKITRTKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAK
ARGDLGAFSRGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE
3D structure
PDB
7f0m
Computational and Structure-Based Development of High Potent Cell-Active Covalent Inhibitor Targeting the Peptidyl-Prolyl Isomerase NIMA-Interacting-1 (Pin1).
Chain
C
Resolution
1.9 Å
3D
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
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
0BF
C
E12 Y23 F25 H27 N30
E7 Y18 F20 H22 N25
BS02
0BF
C
L61 C113 M130 Q131 F134 S154
L44 C96 M113 Q114 F117 S137
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
View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB
RCSB:7f0m
,
PDBe:7f0m
,
PDBj:7f0m
PDBsum
7f0m
PubMed
35089030
UniProt
Q13526
|PIN1_HUMAN Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Gene Name=PIN1)
[
Back to BioLiP
]