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6MNH

ULK1 Unc-51 like autophagy activating kinase in complex with inhibitor BTC

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
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue JVD A 301
ChainResidue
AGLY23
AHOH423
AHOH539
AHIS24
AALA44
ALYS46
AVAL76
AGLU93
ACYS95
AGLN142
ALEU145

site_idAC2
Number of Residues3
Detailsbinding site for residue DMS A 302
ChainResidue
AMET107
ATHR114
ASER158

site_idAC3
Number of Residues3
Detailsbinding site for residue CL A 303
ChainResidue
AHIS105
AARG108
ALYS286

site_idAC4
Number of Residues2
Detailsbinding site for residue CL A 304
ChainResidue
AARG108
AGLN227

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues25
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGHGAFAVVFkGrhrekhdle.........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 Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP138

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AILE22

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000305|PubMed:20921139
ChainResidueDetails
ALYS46

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:O70405
ChainResidueDetails
ALYS162

222624

PDB entries from 2024-07-17

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