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1TQP

Crystal Structure of A. fulgidus Rio2 Serine Protein Kinase Bound to ATP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0006338biological_processchromatin remodeling
A0006468biological_processprotein phosphorylation
A0016310biological_processphosphorylation
A0030490biological_processmaturation of SSU-rRNA
A0030688cellular_componentpreribosome, small subunit precursor
A0044024molecular_functionhistone H2AS1 kinase activity
A0046872molecular_functionmetal ion binding
A0106310molecular_functionprotein serine kinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE ATP A 283
ChainResidue
AMSE98
AILE182
AGLU186
ATYR222
AASN223
AILE234
AASP235
AHOH285
AHOH307
AHOH367
AHOH402
AGLY101
AHOH409
ALYS102
AGLU103
ASER104
ALYS120
APRO167
AMSE179
AGLU180

Functional Information from PROSITE/UniProt
site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. IVHgDLSQYNVLV
ChainResidueDetails
AILE214-VAL226

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AASP218

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AMSE98

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305|PubMed:15943813
ChainResidueDetails
AGLU103
AASN223
AASP235

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:15341724
ChainResidueDetails
ALYS120

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:15943813, ECO:0007744|PDB:1ZAO
ChainResidueDetails
AHIS126

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:15341724, ECO:0000269|PubMed:15943813, ECO:0007744|PDB:1TQP, ECO:0007744|PDB:1ZAO
ChainResidueDetails
AGLU180

site_idSWS_FT_FI7
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:15341724, ECO:0007744|PDB:1TQP
ChainResidueDetails
ATYR222

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:15943813
ChainResidueDetails
ASER128

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 2phk
ChainResidueDetails
AASP218
ASER220

223790

PDB entries from 2024-08-14

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