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2VZ6

Structure of human calcium calmodulin dependent protein kinase type II alpha (CAMK2A) in complex with Indirubin E804

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 Residues10
DetailsBINDING SITE FOR RESIDUE FEF A 600
ChainResidue
ALEU19
AASP156
AALA40
APHE89
AASP90
ALEU91
AVAL92
AGLU139
AASN140
ALEU142

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE FEF B 600
ChainResidue
BLEU19
BALA40
BPHE89
BASP90
BLEU91
BVAL92
BGLU139
BLEU142
BASP156

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PGO A 1301
ChainResidue
AGLN117
AILE271
AHIS273
AARG274
ASER275
APGO1302
AHOH2146
BSER108
BALA110
BASP111

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PGO A 1302
ChainResidue
AARG274
ASER275
APGO1301
AHOH2147
BCYS280

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PGO B 1302
ChainResidue
AARG52
AGLN55
BGLU236
BGLU285
BCYS289
BHOH2111

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

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VvHrDLKpeNLLL
ChainResidueDetails
AVAL131-LEU143

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
AASP135
BASP135

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU19
ALYS42
BLEU19
BLYS42

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P11798
ChainResidueDetails
ATYR13
BTYR13

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P11275
ChainResidueDetails
ASER257
BSER257

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000250|UniProtKB:P11275
ChainResidueDetails
ATHR286
BTHR286

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP135
AGLU139

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP135
BGLU139

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP135
ALYS137

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP135
BLYS137

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP135
ALYS137
ATHR176

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP135
BLYS137
BTHR176

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP135
AASN140
ALYS137

site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP135
BASN140
BLYS137

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PDB entries from 2024-07-24

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