Structure of PDB 8sg2 Chain A Binding Site BS01

Receptor Information
>8sg2 Chain A (length=163) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MADEEKLPPGWEKRMSRSSGRVYYFNHITNASQWERPSGNSSSGGKNGQG
EPARVRCSHLLVKHSQSRRPSSWRQEKITRTKEEALELINGYIQKIKSGE
EDFESLASQFSDCSSAKARGDLGAFSRGQMQKPFEDASFALRTGEMSGPV
FTDSGIHIILRTE
Ligand information
>8sg2 Chain B (length=23) Species: 9606 (Homo sapiens) [Search peptide sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
VLTPPDQEVIRNIDQSEFEGFSF
Receptor-Ligand Complex Structure
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PDB8sg2 A novel bivalent interaction mode underlies a non-catalytic mechanism for Pin1-mediated protein kinase C regulation.
ResolutionN/A
Binding residue
(original residue number in PDB)		S16 R17 F25 T29 N30 A31 S32 W34 V55 C57 H59 R68 R69 N90 I93 Q94 L122 F125 Q129 M130 Q131 F134 A137 S138 A140 L141 S147 G148 V150 T152 D153 S154 H157 I159
Binding residue
(residue number reindexed from 1)		S16 R17 F25 T29 N30 A31 S32 W34 V55 C57 H59 R68 R69 N90 I93 Q94 L122 F125 Q129 M130 Q131 F134 A137 S138 A140 L141 S147 G148 V150 T152 D153 S154 H157 I159
Enzymatic activity
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:8sg2, PDBe:8sg2, PDBj:8sg2
PDBsum8sg2
PubMed38687676
UniProtQ13526|PIN1_HUMAN Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Gene Name=PIN1)

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