Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

7B55

Crystal structure of CaMKII-actinin complex bound to MES

Functional Information from GO Data
ChainGOidnamespacecontents
B0004672molecular_functionprotein kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue MES B 401
ChainResidue
BALA40
BLYS42
BVAL73
BPHE89
BASP90
BVAL92
BALA155
BASP156
BHOH638

site_idAC2
Number of Residues8
Detailsbinding site for residue MES B 402
ChainResidue
BLYS250
BSER257
BLYS258
BARG259
BILE260
BGLU264
BHOH518
BHOH655

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGAFSVVRrCvkvlagqe..........YAAK
ChainResidueDetails
BLEU19-LYS42

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VvHrDLKpeNLLL
ChainResidueDetails
BVAL131-LEU143

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
BASP135

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
BLYS42
BLEU19

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18034455
ChainResidueDetails
BTYR13

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P11275
ChainResidueDetails
BSER257

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:28130356
ChainResidueDetails
BTHR286

220472

PDB entries from 2024-05-29

PDB statisticsPDBj update infoContact PDBjnumon