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4YVC

ROCK 1 bound to thiazole inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0004674molecular_functionprotein serine/threonine kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue 4KH A 501
ChainResidue
AILE82
AASP216
AGLY83
AARG84
APHE87
AVAL90
AALA103
ALYS105
AGLU154
AMET156

site_idAC2
Number of Residues10
Detailsbinding site for residue 4KH B 501
ChainResidue
BILE82
BGLY83
BARG84
BPHE87
BVAL90
BLYS105
BMET153
BGLU154
BMET156
BASP216

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGRGAFGEVQlVrhkstrkv..........YAMK
ChainResidueDetails
AILE82-LYS105

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. FiHrDVKpdNMLL
ChainResidueDetails
APHE194-LEU206

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP198
BASP198

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AILE82
ALYS105
BILE82
BLYS105

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PDB entries from 2024-07-24

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