Structure of PDB 2esm Chain A Binding Site BS01

Receptor Information
>2esm Chain A (length=400) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SFETRFEKMDNLLRDPKSEVNSDCLLDGLDALVYDLDFPALRKNKNIDNF
LSRYKDTINKIRDLRMKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMK
LLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEY
MPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNML
LDKSGHLKLADFGTCMKMNKEGMVRCDTAVGTPDYISPEVLKSQGGDGYY
GRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDI
SKEAKNLICAFLTDREVRLGRNGVEEIKRHLFFKNDQWAWETLRDTVAPV
VPDLSSDIDTSNFDDLEEDKGEEETFPIPKAFVGNQLPFVGFTYYSNRRY
Ligand information
Ligand IDM77
InChIInChI=1S/C14H17N3O2S/c18-20(19,17-9-2-6-15-8-10-17)14-4-1-3-12-11-16-7-5-13(12)14/h1,3-5,7,11,15H,2,6,8-10H2
InChIKeyNGOGFTYYXHNFQH-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 12.01O=S(=O)(c2c1ccncc1ccc2)N3CCCNCC3
CACTVS 3.370O=[S](=O)(N1CCCNCC1)c2cccc3cnccc23
OpenEye OEToolkits 1.7.2c1cc2cnccc2c(c1)S(=O)(=O)N3CCCNCC3
FormulaC14 H17 N3 O2 S
Name5-(1,4-DIAZEPAN-1-SULFONYL)ISOQUINOLINE;
Fasudil;
(5-ISOQUINOLINESULFONYL)HOMOPIPERAZINE
ChEMBLCHEMBL38380
DrugBankDB08162
ZINCZINC000000006486
PDB chain2esm Chain A Residue 416 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB2esm The Structure of Dimeric ROCK I Reveals the Mechanism for Ligand Selectivity.
Resolution3.2 Å
Binding residue
(original residue number in PDB)		I82 V90 A103 M153 Y155 M156 D160 D202 L205 F368
Binding residue
(residue number reindexed from 1)		I77 V85 A98 M148 Y150 M151 D155 D197 L200 F363
Annotation score1
Binding affinityBindingDB: Ki=530nM,IC50=180nM
Enzymatic activity
Catalytic site (original residue number in PDB) D198 K200 N203 D216 T237
Catalytic site (residue number reindexed from 1) D193 K195 N198 D211 T232
Enzyme Commision number 2.7.11.1: non-specific serine/threonine protein kinase.
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2esm, PDBe:2esm, PDBj:2esm
PDBsum2esm
PubMed16249185
UniProtQ13464|ROCK1_HUMAN Rho-associated protein kinase 1 (Gene Name=ROCK1)

[Back to BioLiP]