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5UZJ

Crystal Structure of ROCK1 bound to an aminopyridine 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 Residues17
Detailsbinding site for residue 8UV A 501
ChainResidue
AILE82
ALEU107
AGLU154
ATYR155
AMET156
ALEU205
AALA215
AASP216
APHE368
AGLY85
AALA86
APHE87
AGLY88
AGLU89
AVAL90
AALA103
ALYS105

site_idAC2
Number of Residues16
Detailsbinding site for residue 8UV B 501
ChainResidue
BILE82
BGLY85
BGLY88
BGLU89
BVAL90
BALA103
BLYS105
BLEU107
BMET153
BGLU154
BTYR155
BMET156
BLEU205
BALA215
BASP216
BPHE368

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

218853

PDB entries from 2024-04-24

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