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3TAC

Crystal Structure of the Liprin-alpha/CASK complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 346
ChainResidue
AARG106
APHE111
AASN154

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 347
ChainResidue
ASO4348
ALYS143
APRO144
AHIS145
APHE185
APHE298
AARG302

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 348
ChainResidue
AHIS184
APHE185
APHE298
ASO4347

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 1
ChainResidue
BHOH23
BARG1095
BGLN1099
BSER1109
BASP1111
BARG1112
BARG1115

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 3
ChainResidue
BHOH70
BSER935
BARG955

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 4
ChainResidue
BPRO914
BALA915

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 5
ChainResidue
BARG1083
BLEU1084
BARG1094
BLEU1106

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 1194
ChainResidue
BARG1123

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues264
DetailsDomain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues10
DetailsRegion: {"description":"Calmodulin-binding"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00100","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"18423203","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"O70589","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues66
DetailsDomain: {"description":"SAM 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00184","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues64
DetailsDomain: {"description":"SAM 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00184","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues69
DetailsDomain: {"description":"SAM 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00184","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues26
DetailsCoiled coil: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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