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7B8W

Structure of LIMK1 Kinase domain with allosteric inhibitor TH-470

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
C0004672molecular_functionprotein kinase activity
C0005524molecular_functionATP binding
C0006468biological_processprotein phosphorylation
D0004672molecular_functionprotein kinase activity
D0005524molecular_functionATP binding
D0006468biological_processprotein phosphorylation
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGCFGQAIkVthretgev..........MVMK
ChainResidueDetails
ALEU345-LYS368

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
AASP460
BASP460
CASP460
DASP460

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU345
ALYS368
BLEU345
BLYS368
CLEU345
CLYS368
DLEU345
DLYS368

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976
ChainResidueDetails
ASER337
BSER337
CSER337
DSER337

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphothreonine; by ROCK1 and PAK1 => ECO:0000269|PubMed:10559936, ECO:0000269|PubMed:10652353, ECO:0000269|PubMed:15660133, ECO:0000269|PubMed:23633677
ChainResidueDetails
ATHR508
BTHR508
CTHR508
DTHR508

222624

PDB entries from 2024-07-17

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