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4GUE

Structure of N-terminal kinase domain of RSK2 with flavonoid glycoside quercitrin

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE QCT A 401
ChainResidue
APHE79
ALEU214
AHOH513
AHOH530
AHOH584
AHOH615
AHOH623
AHOH694
AHOH729
AALA98
ALYS100
AVAL131
ALEU147
AASP148
ALEU155
AGLU197
ALEU200

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 402
ChainResidue
AHIS60
ALYS62
AALA63
ATYR135
AALA136

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 403
ChainResidue
AILE330
AILE330
AASP331
AASP331
ATRP332
ATRP332
AHOH625
AHOH625
AHOH743
AHOH743

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues27
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGQGSFGKVFlVkkisgsdarql.......YAMK
ChainResidueDetails
ALEU74-LYS100

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiYrDLKpeNILL
ChainResidueDetails
AILE189-LEU201

site_idPS00284
Number of Residues11
DetailsSERPIN Serpins signature. VEVNHPFIVkL
ChainResidueDetails
AVAL123-LEU133

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
AASP193

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALYS100
ALEU74

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PDPK1 => ECO:0000269|PubMed:10480933
ChainResidueDetails
ASER227

221051

PDB entries from 2024-06-12

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