Structure of PDB 8sg2 Chain A

Receptor sequence

>8sg2A (length=163) Species: 9606 (Homo sapiens) [Search protein sequence]

MADEEKLPPGWEKRMSRSSGRVYYFNHITNASQWERPSGNSSSGGKNGQG
EPARVRCSHLLVKHSQSRRPSSWRQEKITRTKEEALELINGYIQKIKSGE
EDFESLASQFSDCSSAKARGDLGAFSRGQMQKPFEDASFALRTGEMSGPV
FTDSGIHIILRTE

3D structure

PDB

8sg2 A novel bivalent interaction mode underlies a non-catalytic mechanism for Pin1-mediated protein kinase C regulation.

Chain

Resolution

N/A

3D
structure

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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	peptide	A	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	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

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
PDBsum	8sg2
PubMed	38687676
UniProt	Q13526\|PIN1_HUMAN Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Gene Name=PIN1)

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