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6YID

Crystal structure of ULK2 in complex with SBI-0206965

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 Residues8
Detailsbinding site for residue EDJ A 301
ChainResidue
AVAL15
ALYS39
AMET85
AGLU86
ATYR87
ACYS88
AGLY91
AASN136

site_idAC2
Number of Residues9
Detailsbinding site for residue EDJ B 301
ChainResidue
BVAL23
BALA37
BLYS39
BGLU86
BCYS88
BGLY91
BASP92
BGLN135
BVAL15

site_idAC3
Number of Residues7
Detailsbinding site for residue EDJ C 301
ChainResidue
CVAL15
CALA37
CLYS39
CGLU86
CCYS88
CGLY91
CGLN135

site_idAC4
Number of Residues6
Detailsbinding site for residue EDJ D 301
ChainResidue
DVAL23
DLYS39
DGLU86
DTYR87
DCYS88
DGLY91

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues25
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGHGAFAVVFrGrhrqktdwe.........VAIK
ChainResidueDetails
AVAL15-LYS39

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKpqNILL
ChainResidueDetails
AILE127-LEU139

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
AASP131
BASP131
CASP131
DASP131

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
BVAL15
CVAL15
DVAL15
AVAL15

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
BLYS39
CLYS39
DLYS39
ALYS39

219140

PDB entries from 2024-05-01

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