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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9B9G

Structure of the PI4KA complex bound to Calcineurin

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DLDNSGSLSveEF
ChainResidueDetails
HASP31-PHE43
HASP63-PHE75
HASP100-LEU112
HASP141-PHE153
site_idPS00063
Number of Residues16
DetailsALDOKETO_REDUCTASE_3 Aldo/keto reductase family putative active site signature. LARSLAvqRPaSLeKV
ChainResidueDetails
ALEU38-VAL53
site_idPS00125
Number of Residues6
DetailsSER_THR_PHOSPHATASE Serine/threonine specific protein phosphatases signature. LRGNHE
ChainResidueDetails
ILEU147-GLU152
site_idPS00915
Number of Residues15
DetailsPI3_4_KINASE_1 Phosphatidylinositol 3- and 4-kinases signature 1. FKvg.DDCRQDmlalQ
ChainResidueDetails
APHE1849-GLN1863
site_idPS00916
Number of Residues21
DetailsPI3_4_KINASE_2 Phosphatidylinositol 3- and 4-kinases signature 2. SmAaysLllFLLqIkDRHngN
ChainResidueDetails
ASER1942-ASN1962
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:8524402
ChainResidueDetails
IHIS151
HGLU74
HASP141
HASP143
HASP145
HARG147
HGLU152
JASP31
JASP33
JSER35
JSER37
KHIS151
JGLU42
JASP63
JASP65
JASN67
JGLU69
JGLU74
JASP141
JASP143
JASP145
JARG147
HSER35
JGLU152
HSER37
HGLU42
HASP63
HASP65
HASN67
HGLU69
site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722, ECO:0000269|PubMed:26248042, ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:31375679, ECO:0000269|PubMed:8524402, ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63, ECO:0007744|PDB:2P6B, ECO:0007744|PDB:3LL8, ECO:0007744|PDB:5C1V, ECO:0007744|PDB:5SVE, ECO:0007744|PDB:6NUC, ECO:0007744|PDB:6NUU, ECO:0007744|PDB:6UUQ
ChainResidueDetails
IASP90
KASN150
KHIS429
KHIS511
IHIS92
IASP118
IASN150
IHIS429
IHIS511
KASP90
KHIS92
KASP118
site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Interaction with PxVP motif in substrate => ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:27974827
ChainResidueDetails
ITRP582
KTRP582
JMET118
JASN122
site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0007744|PubMed:22814378
ChainResidueDetails
ISER2
KSER2
site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: 3'-nitrotyrosine => ECO:0000250|UniProtKB:P63328
ChainResidueDetails
ITYR454
KTYR454
site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATYR1154
BTYR1154
site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER1436
BSER1436
Catalytic Information from CSA
site_idMCSA1
Number of Residues10
DetailsM-CSA 406
ChainResidueDetails
IASP90metal ligand
IHIS511metal ligand
IHIS92metal ligand
IASP118metal ligand
IASP121electrostatic stabiliser
IARG122transition state stabiliser
IASN150metal ligand
IHIS151proton shuttle (general acid/base)
IHIS429metal ligand
IARG484transition state stabiliser
site_idMCSA2
Number of Residues10
DetailsM-CSA 406
ChainResidueDetails
KASP90metal ligand
KHIS511metal ligand
KHIS92metal ligand
KASP118metal ligand
KASP121electrostatic stabiliser
KARG122transition state stabiliser
KASN150metal ligand
KHIS151proton shuttle (general acid/base)
KHIS429metal ligand
KARG484transition state stabiliser

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PDB entries from 2024-10-09

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