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

6X5Q

Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and GluA1

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 GOL A 301
ChainResidue
AARG104
ATYR106
ASER108

site_idAC2
Number of Residues6
Detailsbinding site for residue GOL A 302
ChainResidue
AGLU96
APHE98
AGLU99
AGLU139
AHOH426
AHOH478

site_idAC3
Number of Residues7
Detailsbinding site for residue GOL B 901
ChainResidue
ATRP214
AHOH442
BCYS825
BLEU826
BILE827
BGLN829
BHOH1010

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGAFSVVRrCvkvlagqe..........YAAK
ChainResidueDetails
ALEU19-LYS42

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P19490
ChainResidueDetails
BMET821
BALA835

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU19
ALYS42

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P11798
ChainResidueDetails
ATYR13

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P11275
ChainResidueDetails
ASER257

223166

PDB entries from 2024-07-31

PDB statisticsPDBj update infoContact PDBjnumon