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6ED6

Crystal structure of Rock2 with a pyridinylbenzamide based 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 Residues14
Detailsbinding site for residue J0P A 501
ChainResidue
AILE98
ATYR171
AMET172
ALEU221
AASP232
APHE384
AGLY101
AALA102
APHE103
AGLY104
AALA119
ALYS121
ALEU123
AGLU170

site_idAC2
Number of Residues14
Detailsbinding site for residue J0P B 501
ChainResidue
BILE98
BGLY104
BGLU105
BVAL106
BALA119
BLYS121
BLEU123
BPHE136
BGLU170
BTYR171
BMET172
BLEU221
BALA231
BASP232

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGRGAFGEVQlVrhkasqkv..........YAMK
ChainResidueDetails
AILE98-LYS121

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LiHrDVKpdNMLL
ChainResidueDetails
ALEU210-LEU222

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
AASP214
BASP214

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AILE98
ALYS121
BILE98
BLYS121

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by ROCK2 => ECO:0000250|UniProtKB:Q62868
ChainResidueDetails
ATHR414
BTHR414

222036

PDB entries from 2024-07-03

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