Structure of PDB 6p5m Chain B

Receptor sequence
>6p5mB (length=388) Species: 9606 (Homo sapiens) [Search protein sequence]
SPGASRQRKLEALIRDPRSPINVESLLDGLNSLVLDLDFPALRKNKNIDN
FLNRYEKIVKKIRGLQMKAEDYDVVKVIGRGAFGEVQLVRHKASQKVYAM
KLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVME
YMPGGDLVNLMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNM
LLDKHGHLKLADFGTCMKMDETGMVHCDTAVGTPDYISPEVLKSQGGDGY
YGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMDHKNSLCFPEDAE
ISKHAKNLICAFLTDREVRLGRNGVEEIRQHPFFKNDQWHWDNIRETAAP
VVPELSSDIDSSNFDDTFPIPKAFVGNQLPFIGFTYYR
3D structure
PDB6p5m Discovery of a Novel, Highly Potent, and Selective Thieno[3,2-d]pyrimidinone-Based Cdc7 Inhibitor with a Quinuclidine Moiety (TAK-931) as an Orally Active Investigational Antitumor Agent.
ChainB
Resolution2.65 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D214 K216 N219 D232 T253
Catalytic site (residue number reindexed from 1) D194 K196 N199 D212 T233
Enzyme Commision number 2.7.11.1: non-specific serine/threonine protein kinase.
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 O1S B A119 K121 M169 E170 Y171 M172 N219 L221 D232 A99 K101 M149 E150 Y151 M152 N199 L201 D212
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004674 protein serine/threonine kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation

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Molecular Function
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Biological Process
External links
PDB RCSB:6p5m, PDBe:6p5m, PDBj:6p5m
PDBsum6p5m
PubMed31895562
UniProtO75116|ROCK2_HUMAN Rho-associated protein kinase 2 (Gene Name=ROCK2)

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