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4WNP

Structure of ULK1 bound to a potent inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
A0010506biological_processregulation of autophagy
B0004672molecular_functionprotein kinase activity
B0004674molecular_functionprotein serine/threonine kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
B0010506biological_processregulation of autophagy
C0004672molecular_functionprotein kinase activity
C0004674molecular_functionprotein serine/threonine kinase activity
C0005524molecular_functionATP binding
C0006468biological_processprotein phosphorylation
C0010506biological_processregulation of autophagy
D0004672molecular_functionprotein kinase activity
D0004674molecular_functionprotein serine/threonine kinase activity
D0005524molecular_functionATP binding
D0006468biological_processprotein phosphorylation
D0010506biological_processregulation of autophagy
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue GOL A 301
ChainResidue
AHIS130
AILE134
AILE135
ALEU172
APHE269

site_idAC2
Number of Residues7
Detailsbinding site for residue GOL A 302
ChainResidue
AHOH462
BSER131
BGLY133
AHIS130
ASER131
AGLY133
ALEU172

site_idAC3
Number of Residues13
Detailsbinding site for residue 3RJ A 303
ChainResidue
AILE22
AALA44
AGLU93
ATYR94
ACYS95
AASN96
AGLY98
AASP102
AGLN142
AASN143
ALEU145
AHOH425
AHOH460

site_idAC4
Number of Residues10
Detailsbinding site for residue 3RJ B 401
ChainResidue
BILE22
BALA44
BGLU93
BTYR94
BCYS95
BGLY98
BASP99
BGLN142
BASN143
BLEU145

site_idAC5
Number of Residues11
Detailsbinding site for residue 3RJ C 401
ChainResidue
CILE22
CALA44
CGLU93
CTYR94
CCYS95
CASN96
CGLY98
CASP102
CGLN142
CASN143
CLEU145

site_idAC6
Number of Residues12
Detailsbinding site for residue 3RJ D 401
ChainResidue
DILE22
DALA44
DLYS46
DGLU93
DTYR94
DCYS95
DGLY98
DASP99
DGLN142
DASN143
DLEU145
DHOH539

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues25
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGHGAFAVVFkGrhraahdle.........VAVK
ChainResidueDetails
AILE22-LYS46

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKpqNILL
ChainResidueDetails
AILE134-LEU146

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
AASP138
BASP138
CASP138
DASP138

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AILE22
BILE22
CILE22
DILE22

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000305|PubMed:20921139
ChainResidueDetails
ALYS46
BLYS46
CLYS46
DLYS46

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:O70405
ChainResidueDetails
ALYS162
BLYS162
CLYS162
DLYS162

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PDB entries from 2024-07-10

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