Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6MXG

Crystal structure of Trypanosoma brucei hypoxanthine-guanine phosphoribosyltranferase in complex with XMP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0004422molecular_functionhypoxanthine phosphoribosyltransferase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006166biological_processpurine ribonucleoside salvage
A0006178biological_processguanine salvage
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0020015cellular_componentglycosome
A0031981cellular_componentnuclear lumen
A0032263biological_processGMP salvage
A0032264biological_processIMP salvage
A0046100biological_processhypoxanthine metabolic process
A0046872molecular_functionmetal ion binding
A0052657molecular_functionguanine phosphoribosyltransferase activity
A0097014cellular_componentciliary plasm
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0004422molecular_functionhypoxanthine phosphoribosyltransferase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006166biological_processpurine ribonucleoside salvage
B0006178biological_processguanine salvage
B0016740molecular_functiontransferase activity
B0016757molecular_functionglycosyltransferase activity
B0020015cellular_componentglycosome
B0031981cellular_componentnuclear lumen
B0032263biological_processGMP salvage
B0032264biological_processIMP salvage
B0046100biological_processhypoxanthine metabolic process
B0046872molecular_functionmetal ion binding
B0052657molecular_functionguanine phosphoribosyltransferase activity
B0097014cellular_componentciliary plasm
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue XMP A 301
ChainResidue
AGLU113
APHE166
AVAL167
ALEU172
AASP173
ASO4304
AHOH403
AILE115
AASP117
ATHR118
AALA119
ALEU120
ATHR121
ALEU122
ALYS145

site_idAC2
Number of Residues3
Detailsbinding site for residue MG A 302
ChainResidue
AASP34
AHOH412
AHOH420

site_idAC3
Number of Residues2
Detailsbinding site for residue MG A 303
ChainResidue
AHOH422
AHOH428

site_idAC4
Number of Residues3
Detailsbinding site for residue SO4 A 304
ChainResidue
ALEU53
AASP173
AXMP301

site_idAC5
Number of Residues15
Detailsbinding site for residue XMP B 301
ChainResidue
BILE115
BASP117
BTHR118
BLYS145
BPHE166
BVAL167
BVAL168
BLEU172
BASP173
BMG302
BMG303
BSO4304
BHOH401
BHOH402
BHOH423

site_idAC6
Number of Residues4
Detailsbinding site for residue MG B 302
ChainResidue
BASP173
BXMP301
BSO4304
BHOH402

site_idAC7
Number of Residues4
Detailsbinding site for residue MG B 303
ChainResidue
BLEU53
BGLU113
BASP114
BXMP301

site_idAC8
Number of Residues8
Detailsbinding site for residue SO4 B 304
ChainResidue
BLEU53
BLYS54
BGLY55
BASP173
BARG179
BXMP301
BMG302
BHOH419

Functional Information from PROSITE/UniProt
site_idPS00103
Number of Residues13
DetailsPUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. VLVLEDILDTAlT
ChainResidueDetails
AVAL109-THR121

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues22
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

PDB statisticsPDBj update infoContact PDBjnumon