Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5YW5

Crystal structure of Adenine phosphoribosyltransferase from Francisella tularensis in complex with adenine

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 Residues4
Detailsbinding site for residue ADE A 201
ChainResidue
AMET22
APHE23
AARG24
ALEU155

site_idAC2
Number of Residues3
Detailsbinding site for residue ADE B 201
ChainResidue
BMET22
BPHE23
BARG24

site_idAC3
Number of Residues4
Detailsbinding site for residue ADE C 201
ChainResidue
CARG24
CLEU125
CMET22
CPHE23

site_idAC4
Number of Residues4
Detailsbinding site for residue ADE D 201
ChainResidue
DMET22
DPHE23
DARG24
DLEU125

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

221716

PDB entries from 2024-06-26

PDB statisticsPDBj update infoContact PDBjnumon