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6AYW

The structure of human CamKII with bound inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue C2V A 401
ChainResidue
ALEU20
ALEU143
AASP157
AVAL28
AALA41
AVAL74
APHE90
AASP91
AVAL93
AGLU140
AASN141

site_idAC2
Number of Residues7
Detailsbinding site for residue DTT A 402
ChainResidue
AGLN118
AILE272
ACYS273
AGLN274
AARG275
ASER276
AHOH623

site_idAC3
Number of Residues6
Detailsbinding site for residue DTT B 401
ChainResidue
BGLN118
BILE272
BCYS273
BGLN274
BARG275
BSER276

site_idAC4
Number of Residues13
Detailsbinding site for residue C2V B 402
ChainResidue
BLEU20
BGLY21
BVAL28
BALA41
BPHE90
BASP91
BLEU92
BVAL93
BGLU140
BASN141
BLEU143
BASP157
BHOH508

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGAFSVVRrCmkiptgqe..........YAAK
ChainResidueDetails
ALEU20-LYS43

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDLKpeNLLL
ChainResidueDetails
AILE132-LEU144

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP136
BASP136

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU20
ALYS43
BLEU20
BLYS43

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:16690701
ChainResidueDetails
ATHR287
BTHR287

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PDB entries from 2024-07-10

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