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5AX9

Crystal structure of the kinase domain of human TRAF2 and NCK-interacting protein kinase in complex with compund 9

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
C0004672molecular_functionprotein kinase activity
C0005524molecular_functionATP binding
C0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue 4KT A 401
ChainResidue
AVAL31
AVAL170
AASP171
AALA52
ALYS54
AGLU106
APHE107
ACYS108
AGLY109
AASP115
ALEU160

site_idAC2
Number of Residues2
Detailsbinding site for residue SO4 A 402
ChainResidue
AASP20
BARG247

site_idAC3
Number of Residues13
Detailsbinding site for residue 4KT B 401
ChainResidue
BVAL31
BVAL39
BALA52
BLYS54
BMET105
BGLU106
BPHE107
BCYS108
BGLY109
BASP115
BGLN157
BLEU160
BASP171

site_idAC4
Number of Residues3
Detailsbinding site for residue SO4 B 402
ChainResidue
BARG19
BASP20
BLYS92

site_idAC5
Number of Residues13
Detailsbinding site for residue 4KT C 401
ChainResidue
CVAL31
CVAL39
CALA52
CLYS54
CGLU106
CPHE107
CCYS108
CGLY109
CASP115
CGLN157
CLEU160
CVAL170
CASP171

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGNGTYGQVYkGrhvktgql..........AAIK
ChainResidueDetails
AVAL31-LYS54

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ViHrDIKgqNVLL
ChainResidueDetails
AVAL149-LEU161

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP153
BASP153
CASP153

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AVAL31
ALYS54
BVAL31
BLYS54
CVAL31
CLYS54

site_idSWS_FT_FI3
Number of Residues3
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P83510
ChainResidueDetails
ATHR187
BTHR187
CTHR187

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PDB entries from 2024-07-24

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