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1ZAO

Crystal Structure of A.fulgidus Rio2 Kinase Complexed With ATP and Manganese Ions

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0006468biological_processprotein phosphorylation
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0016740molecular_functiontransferase activity
A0030490biological_processmaturation of SSU-rRNA
A0030688cellular_componentpreribosome, small subunit precursor
A0046872molecular_functionmetal ion binding
A0106310molecular_functionprotein serine kinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 283
ChainResidue
AASN223
AASP235
AMN284
APO4285
AATP286
AHOH615

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 284
ChainResidue
APO4285
AATP286
AHOH315
AGLU103
AASP235
AMN283

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 A 285
ChainResidue
AGLU103
AASP218
AASN223
AASP235
AMN283
AMN284
AATP286
AHOH309

site_idAC4
Number of Residues24
DetailsBINDING SITE FOR RESIDUE ATP A 286
ChainResidue
AGLU103
ASER104
AVAL106
AVAL118
ALYS120
AHIS122
AHIS126
AMET179
AGLU180
AILE182
AGLU186
AASN223
AILE234
AASP235
APRO237
AMN283
AMN284
APO4285
AHOH294
AHOH303
AHOH337
AHOH350
AHOH529
AHOH586

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 287
ChainResidue
AGLN162
AGLY163
ALEU164
AVAL166
ALYS168

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
AMET98

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

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PDB entries from 2024-04-24

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