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4W7P

Crystal Structure of ROCK 1 bound to YB-15-QD37

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
C0004672molecular_functionprotein kinase activity
C0004674molecular_functionprotein serine/threonine kinase activity
C0005524molecular_functionATP binding
C0006468biological_processprotein phosphorylation
D0004672molecular_functionprotein kinase activity
D0004674molecular_functionprotein serine/threonine kinase activity
D0005524molecular_functionATP binding
D0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue 3J7 A 501
ChainResidue
AILE82
AASP202
ALEU205
AASP216
APHE368
AVAL90
AALA103
ALYS105
AVAL137
AGLU154
ATYR155
AMET156
AASP160

site_idAC2
Number of Residues11
Detailsbinding site for residue 3J7 B 501
ChainResidue
BILE82
BVAL90
BALA103
BLYS105
BGLU154
BTYR155
BMET156
BASP160
BASP202
BASP216
BPHE368

site_idAC3
Number of Residues11
Detailsbinding site for residue 3J7 C 501
ChainResidue
CVAL90
CALA103
CLYS105
CVAL137
CGLU154
CTYR155
CMET156
CASP160
CASP202
CASP216
CPHE368

site_idAC4
Number of Residues11
Detailsbinding site for residue 3J7 D 501
ChainResidue
DVAL90
DALA103
DLYS105
DVAL137
DGLU154
DTYR155
DMET156
DASP160
DASP202
DLEU205
DASP216

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 Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP198
BASP198
CASP198
DASP198

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
CILE82
CLYS105
DILE82
DLYS105
AILE82
ALYS105
BILE82
BLYS105

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: N-acetylserine => ECO:0000269|Ref.4, ECO:0007744|PubMed:22814378
ChainResidueDetails
ASER2
BSER2
CSER2
DSER2

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PDB entries from 2024-05-15

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