Structure of PDB 2v55 Chain C

Receptor sequence
>2v55C (length=396) Species: 9606 (Homo sapiens) [Search protein sequence]
SFETRFEKMDNLLRDPKSEVNSDCLLDGLDALVYDLDFPALRKNKNIDNF
LSRYKDTINKIRDLRMKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMK
LLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEY
MPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNML
LDKSGHLKLADFGTCMKMNKEGMVRCDTAVGTPDYISPEVLKSQGGDGYY
GRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDI
SKEAKNLICAFLTDREVRLGRNGVEEIKRHLFFKNDQWAWETLRDTVAPV
VPDLSSDIDTSNFDDLKGEEETFPIPKAFVGNQLPFVGFTYYSNRR
3D structure
PDB2v55 Mechanism of Multi-Site Phosphorylation from a Rock-I:Rhoe Complex Structure.
ChainC
Resolution3.705 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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.
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 ANP C A86 K105 M153 M156 K200 D202 D216 A81 K100 M148 M151 K195 D197 D211
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:2v55, PDBe:2v55, PDBj:2v55
PDBsum2v55
PubMed18946488
UniProtQ13464|ROCK1_HUMAN Rho-associated protein kinase 1 (Gene Name=ROCK1)

[Back to BioLiP]