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4EQU

Human STK-10 (LOK) kinase domain in DFG-out conformation with inhibitor DSA-7

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 Residues16
DetailsBINDING SITE FOR RESIDUE G6I A 401
ChainResidue
AALA63
AHIS155
ALEU164
ALEU173
AALA174
AASP175
APHE176
ALYS181
AGLU81
ALEU85
AILE93
AVAL94
AILE110
AGLU111
APHE112
ACYS113

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 402
ChainResidue
AGLU313
AGLU316
AHOH509
AHOH510

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 403
ChainResidue
AGLU234
AHOH519
AHOH520
AHOH522
AHOH523

site_idAC4
Number of Residues17
DetailsBINDING SITE FOR RESIDUE G6I B 401
ChainResidue
BALA63
BLYS65
BGLU81
BLEU85
BILE93
BVAL94
BILE110
BGLU111
BPHE112
BCYS113
BGLY116
BLEU164
BLEU173
BALA174
BASP175
BPHE176
BLYS181

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA B 402
ChainResidue
BGLU313
BGLU316
BHOH526

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CA B 403
ChainResidue
BGLU168
BHOH527

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 404
ChainResidue
BGLU234
BHOH530
BHOH531
BHOH533
BHOH534

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE 1PE B 405
ChainResidue
BMET205
BMET209
BALA250

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

223532

PDB entries from 2024-08-07

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