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4HND

Crystal structure of the catalytic domain of Selenomethionine substituted human PI4KIIalpha in complex with ADP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004430molecular_function1-phosphatidylinositol 4-kinase activity
B0004430molecular_function1-phosphatidylinositol 4-kinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE ADP A 500
ChainResidue
AGLY133
AVAL264
AILE345
AASP346
ASER134
ASER137
APHE139
AVAL150
ALYS152
AGLN261
ALEU262
APHE263

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ADP B 500
ChainResidue
BSER137
BLYS152
BGLN261
BLEU262
BPHE263
BVAL264
BILE345
BASP346

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsRegion: {"description":"G-loop","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsRegion: {"description":"Important for substrate binding","evidences":[{"source":"PubMed","id":"24675427","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues34
DetailsRegion: {"description":"Important for interaction with membranes","evidences":[{"source":"PubMed","id":"24675427","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues16
DetailsRegion: {"description":"Catalytic loop","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues40
DetailsRegion: {"description":"Activation loop","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues22
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24675427","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25168678","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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