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4AOT

Crystal Structure of Human Serine Threonine Kinase-10 (LOK) Bound to GW830263A

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 Residues2
DetailsBINDING SITE FOR RESIDUE CL A 1315
ChainResidue
AARG244
ALYS248

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 1316
ChainResidue
ALYS217

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 1317
ChainResidue
AHOH2069

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 1316
ChainResidue
BARG244

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 1318
ChainResidue
ATYR100

site_idAC6
Number of Residues15
DetailsBINDING SITE FOR RESIDUE GW8 A 1319
ChainResidue
ATYR78
AILE108
AILE110
AGLU111
APHE112
ACYS113
AALA117
AALA120
ALEU164
AASP175
APHE176
AHOH2026
ALEU42
AALA63
ALYS65

site_idAC7
Number of Residues13
DetailsBINDING SITE FOR RESIDUE GW8 B 1319
ChainResidue
BLEU42
BALA63
BLYS65
BILE67
BTYR78
BILE108
BILE110
BGLU111
BPHE112
BCYS113
BLEU164
BASP175
BPHE176

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGDGAFGKVYkAknketgal..........AAAK
ChainResidueDetails
ALEU42-LYS65

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKagNVLM
ChainResidueDetails
AILE153-MET165

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
AASP157
BASP157

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU42
BLEU42

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
ALYS65
BLYS65

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:E9PTG8
ChainResidueDetails
ASER20
BSER20

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195
ChainResidueDetails
ASER191
BSER191

218853

PDB entries from 2024-04-24

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