Structure of PDB 5u7r Chain A

Receptor sequence
>5u7rA (length=387) Species: 9606 (Homo sapiens) [Search protein sequence]
SRQRKLEALIRDPRSPINVESLLDGLNSLVLDLDFPALRKNKNIDNFLNR
YEKIVKKIRGLQMKAEDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLS
KFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPG
GDLVNLMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDK
HGHLKLADFGTCMKMDETGMVHCDTAVGTPDYISPEVLKSQGGDGYYGRE
CDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMDHKNSLCFPEDAEISKH
AKNLICAFLTDREVRLGRNGVEEIRQHPFFKNDQWHWDNIRETAAPVVPE
LSSDIDSSNFDDIEETFPIPKAFVGNQLPFIGFTYYR
3D structure
PDB5u7r Identification of a new class of potent Cdc7 inhibitors designed by putative pharmacophore model: Synthesis and biological evaluation of 2,3-dihydrothieno[3,2-d]pyrimidin-4(1H)-ones.
ChainA
Resolution3.33 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) D190 K192 N195 D208 T229
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 81G A A119 K121 M169 M172 D218 L221 D232 F384 A95 K97 M145 M148 D194 L197 D208 F360
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:5u7r, PDBe:5u7r, PDBj:5u7r
PDBsum5u7r
PubMed28284870
UniProtO75116|ROCK2_HUMAN Rho-associated protein kinase 2 (Gene Name=ROCK2)

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