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3BF5

Crystal structure of putative ribokinase (10640157) from Thermoplasma acidophilum at 1.91 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004001molecular_functionadenosine kinase activity
A0005524molecular_functionATP binding
A0005525molecular_functionGTP binding
A0005829cellular_componentcytosol
A0006167biological_processAMP biosynthetic process
A0008617biological_processguanosine metabolic process
A0008906molecular_functioninosine kinase activity
A0009165biological_processnucleotide biosynthetic process
A0009224biological_processCMP biosynthetic process
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0019206molecular_functionnucleoside kinase activity
A0043771molecular_functioncytidine kinase activity
A0046085biological_processadenosine metabolic process
A0046087biological_processcytidine metabolic process
A0046102biological_processinosine metabolic process
A0106366molecular_functionguanosine kinase activity
A1901293biological_processnucleoside phosphate biosynthetic process
A1905108molecular_functionguanosine binding
B0004001molecular_functionadenosine kinase activity
B0005524molecular_functionATP binding
B0005525molecular_functionGTP binding
B0005829cellular_componentcytosol
B0006167biological_processAMP biosynthetic process
B0008617biological_processguanosine metabolic process
B0008906molecular_functioninosine kinase activity
B0009165biological_processnucleotide biosynthetic process
B0009224biological_processCMP biosynthetic process
B0016301molecular_functionkinase activity
B0016310biological_processphosphorylation
B0019206molecular_functionnucleoside kinase activity
B0043771molecular_functioncytidine kinase activity
B0046085biological_processadenosine metabolic process
B0046087biological_processcytidine metabolic process
B0046102biological_processinosine metabolic process
B0106366molecular_functionguanosine kinase activity
B1901293biological_processnucleoside phosphate biosynthetic process
B1905108molecular_functionguanosine binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 B 288
ChainResidue
AARG241
ASER242
ALYS245
BARG241
BSER242
BLYS245
BHOH358

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PGO A 288
ChainResidue
AALA112
AGLY130
AGLU151
ALYS154
AGLN108
AMSE111

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PGO B 289
ChainResidue
BTHR64
BSER89
BHOH301

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PGO B 290
ChainResidue
BMSE62
BGLU73
BASP271
BARG274

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PGO A 289
ChainResidue
AGLN150
AASN173
AHIS175
AGLU176

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PGO B 291
ChainResidue
BPRO189
BMSE206
BASP207
BGLY208
BHOH355

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PGO A 290
ChainResidue
ATHR196
AGLY198
AGLY201
APHE229
AHOH295
AHOH406

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PGO B 292
ChainResidue
BTYR168
BTHR192
BMSE206
BILE243
BHOH356

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:Q57849
ChainResidueDetails
AASP227
BASP227

site_idSWS_FT_FI2
Number of Residues20
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q57849
ChainResidueDetails
AGLY38
AASN42
AGLN102
ASER104
AGLN150
AASN173
ATHR196
AASP227
BASP13
BASN28
BGLY38
BASN42
BGLN102
BSER104
BGLN150
BASN173
BTHR196
BASP227
AASP13
AASN28

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000250|UniProtKB:Q57849
ChainResidueDetails
AARG230
BARG230

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PDB entries from 2024-06-12

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