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

3KB8

2.09 Angstrom resolution structure of a hypoxanthine-guanine phosphoribosyltransferase (hpt-1) from Bacillus anthracis str. 'Ames Ancestor' in complex with GMP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004422molecular_functionhypoxanthine phosphoribosyltransferase activity
A0005737cellular_componentcytoplasm
A0006166biological_processpurine ribonucleoside salvage
A0016757molecular_functionglycosyltransferase activity
A0032264biological_processIMP salvage
A0046872molecular_functionmetal ion binding
A0052657molecular_functionguanine phosphoribosyltransferase activity
B0000166molecular_functionnucleotide binding
B0004422molecular_functionhypoxanthine phosphoribosyltransferase activity
B0005737cellular_componentcytoplasm
B0006166biological_processpurine ribonucleoside salvage
B0016757molecular_functionglycosyltransferase activity
B0032264biological_processIMP salvage
B0046872molecular_functionmetal ion binding
B0052657molecular_functionguanine phosphoribosyltransferase activity
C0000166molecular_functionnucleotide binding
C0004422molecular_functionhypoxanthine phosphoribosyltransferase activity
C0005737cellular_componentcytoplasm
C0006166biological_processpurine ribonucleoside salvage
C0016757molecular_functionglycosyltransferase activity
C0032264biological_processIMP salvage
C0046872molecular_functionmetal ion binding
C0052657molecular_functionguanine phosphoribosyltransferase activity
D0000166molecular_functionnucleotide binding
D0004422molecular_functionhypoxanthine phosphoribosyltransferase activity
D0005737cellular_componentcytoplasm
D0006166biological_processpurine ribonucleoside salvage
D0016757molecular_functionglycosyltransferase activity
D0032264biological_processIMP salvage
D0046872molecular_functionmetal ion binding
D0052657molecular_functionguanine phosphoribosyltransferase activity
Functional Information from PROSITE/UniProt
site_idPS00103
Number of Residues13
DetailsPUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. ILIVEDIIDSGlT
ChainResidueDetails
AILE95-THR107

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a95
ChainResidueDetails
AASP103
AASP100
ALYS131
AGLU99

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a95
ChainResidueDetails
BASP103
BASP100
BLYS131
BGLU99

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a95
ChainResidueDetails
CASP103
CASP100
CLYS131
CGLU99

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a95
ChainResidueDetails
DASP103
DASP100
DLYS131
DGLU99

site_idCSA5
Number of Residues5
DetailsAnnotated By Reference To The Literature 1a95
ChainResidueDetails
AASP103
AARG135
AASP100
ALYS131
AGLU99

site_idCSA6
Number of Residues5
DetailsAnnotated By Reference To The Literature 1a95
ChainResidueDetails
BASP103
BARG135
BASP100
BLYS131
BGLU99

site_idCSA7
Number of Residues5
DetailsAnnotated By Reference To The Literature 1a95
ChainResidueDetails
CASP103
CARG135
CASP100
CLYS131
CGLU99

site_idCSA8
Number of Residues5
DetailsAnnotated By Reference To The Literature 1a95
ChainResidueDetails
DASP103
DARG135
DASP100
DLYS131
DGLU99

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon