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5YW2

Crystal structure of Adenine phosphoribosyltransferase from Francisella tularensis.

Functional Information from GO Data
ChainGOidnamespacecontents
A0002055molecular_functionadenine binding
A0003999molecular_functionadenine phosphoribosyltransferase activity
A0005737cellular_componentcytoplasm
A0006166biological_processpurine ribonucleoside salvage
A0006168biological_processadenine salvage
A0009116biological_processnucleoside metabolic process
A0016208molecular_functionAMP binding
A0016757molecular_functionglycosyltransferase activity
A0044209biological_processAMP salvage
B0002055molecular_functionadenine binding
B0003999molecular_functionadenine phosphoribosyltransferase activity
B0005737cellular_componentcytoplasm
B0006166biological_processpurine ribonucleoside salvage
B0006168biological_processadenine salvage
B0009116biological_processnucleoside metabolic process
B0016208molecular_functionAMP binding
B0016757molecular_functionglycosyltransferase activity
B0044209biological_processAMP salvage
C0002055molecular_functionadenine binding
C0003999molecular_functionadenine phosphoribosyltransferase activity
C0005737cellular_componentcytoplasm
C0006166biological_processpurine ribonucleoside salvage
C0006168biological_processadenine salvage
C0009116biological_processnucleoside metabolic process
C0016208molecular_functionAMP binding
C0016757molecular_functionglycosyltransferase activity
C0044209biological_processAMP salvage
D0002055molecular_functionadenine binding
D0003999molecular_functionadenine phosphoribosyltransferase activity
D0005737cellular_componentcytoplasm
D0006166biological_processpurine ribonucleoside salvage
D0006168biological_processadenine salvage
D0009116biological_processnucleoside metabolic process
D0016208molecular_functionAMP binding
D0016757molecular_functionglycosyltransferase activity
D0044209biological_processAMP salvage
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue SO4 A 201
ChainResidue
ALEU125
ALEU126
AALA127
ATHR128
AGLY129
AGLY130
ATHR131
AALA132
AHOH303

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 202
ChainResidue
AHOH301
AHOH308
AHOH320
AHOH321
AHOH322

site_idAC3
Number of Residues3
Detailsbinding site for residue CL A 203
ChainResidue
ASER62
AARG63
BARG83

site_idAC4
Number of Residues2
Detailsbinding site for residue CL A 204
ChainResidue
AARG83
BARG63

site_idAC5
Number of Residues3
Detailsbinding site for residue CL A 205
ChainResidue
AARG83
BSER62
BARG63

site_idAC6
Number of Residues3
Detailsbinding site for residue CL A 206
ChainResidue
AARG63
AHOH304
BARG83

site_idAC7
Number of Residues8
Detailsbinding site for residue SO4 C 201
ChainResidue
CLEU125
CLEU126
CALA127
CTHR128
CGLY129
CGLY130
CTHR131
CALA132

site_idAC8
Number of Residues2
Detailsbinding site for residue CL C 202
ChainResidue
CSER62
DARG83

site_idAC9
Number of Residues2
Detailsbinding site for residue CL C 203
ChainResidue
CARG63
DARG83

site_idAD1
Number of Residues8
Detailsbinding site for residue SO4 B 201
ChainResidue
BLEU125
BLEU126
BALA127
BTHR128
BGLY129
BGLY130
BTHR131
BALA132

site_idAD2
Number of Residues2
Detailsbinding site for residue CL D 201
ChainResidue
CARG83
DARG63

site_idAD3
Number of Residues8
Detailsbinding site for residue SO4 D 202
ChainResidue
DLEU125
DALA127
DTHR128
DGLY129
DGLY130
DTHR131
DALA132
DHOH301

site_idAD4
Number of Residues5
Detailsbinding site for residue MG D 203
ChainResidue
DHOH302
DHOH303
DHOH310
DHOH311
DHOH313

site_idAD5
Number of Residues3
Detailsbinding site for residue CL D 204
ChainResidue
CARG83
DSER62
DARG63

Functional Information from PROSITE/UniProt
site_idPS00103
Number of Residues13
DetailsPUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. VLVVDDLLATGgT
ChainResidueDetails
AVAL119-THR131

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PDB entries from 2024-10-09

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