Structure of PDB 3tc5 Chain A

Receptor sequence
>3tc5A (length=144) Species: 9606 (Homo sapiens) [Search protein sequence]
LPPGWEKAMSRSSGRVYYFNHITNASQWERPEPARVRCSHLLVKHSQSRR
PSSWRQEKITRTKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKAR
GDLGAFSRGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE
3D structure
PDB3tc5 Selective targeting of disease-relevant protein binding domains by o-phosphorylated natural product derivatives.
ChainA
Resolution1.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H59 C113 Q131 S154 H157
Catalytic site (residue number reindexed from 1) H40 C94 Q112 S135 H138
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 3T5 A K63 R68 R69 F125 Q129 M130 Q131 F134 S154 H157 K44 R49 R50 F106 Q110 M111 Q112 F115 S135 H138 PDBbind-CN: -logKd/Ki=5.17,Kd=6.8uM
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:3tc5, PDBe:3tc5, PDBj:3tc5
PDBsum3tc5
PubMed21797253
UniProtQ13526|PIN1_HUMAN Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Gene Name=PIN1)

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