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5ANL

Crystal structure of VPS34 in complex with (2S)-8-((3R)-3- Methylmorpholin-4-yl)-1-(3-methyl-2-oxo- butyl)-2-(trifluoromethyl)-3, 4-dihydro-2H-pyrimido(1,2-a)pyrimidin-6- one, processed with the CrystalDirect automated mounting and cryo-cooling technology

Functional Information from GO Data
ChainGOidnamespacecontents
A0016301molecular_functionkinase activity
A0046854biological_processphosphatidylinositol phosphate biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE RBQ A 1870
ChainResidue
APHE612
AASP761
APRO618
AILE634
AMET682
AGLN683
APHE684
AILE685
APRO689
AILE760

Functional Information from PROSITE/UniProt
site_idPS00915
Number of Residues15
DetailsPI3_4_KINASE_1 Phosphatidylinositol 3- and 4-kinases signature 1. FKhg.DDLRQDqlilQ
ChainResidueDetails
APHE635-GLN649

site_idPS00916
Number of Residues21
DetailsPI3_4_KINASE_2 Phosphatidylinositol 3- and 4-kinases signature 2. ScAgycVitYILgVgDRHldN
ChainResidueDetails
ASER728-ASN748

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER282

220472

PDB entries from 2024-05-29

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