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

6FD6

Crystal Structure of Human APRT-Tyr105Phe variant in complex with Adenine, PRPP and Mg2+, 30 days post crystallization (with AMP and PPi products fully generated)

Functional Information from GO Data
ChainGOidnamespacecontents
A0002055molecular_functionadenine binding
A0003999molecular_functionadenine phosphoribosyltransferase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006166biological_processpurine ribonucleoside salvage
A0006168biological_processadenine salvage
A0007625biological_processgrooming behavior
A0016208molecular_functionAMP binding
A0016757molecular_functionglycosyltransferase activity
A0032263biological_processGMP salvage
A0032264biological_processIMP salvage
A0034774cellular_componentsecretory granule lumen
A0044209biological_processAMP salvage
A0046083biological_processadenine metabolic process
A0070062cellular_componentextracellular exosome
B0002055molecular_functionadenine binding
B0003999molecular_functionadenine phosphoribosyltransferase activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006166biological_processpurine ribonucleoside salvage
B0006168biological_processadenine salvage
B0007625biological_processgrooming behavior
B0016208molecular_functionAMP binding
B0016757molecular_functionglycosyltransferase activity
B0032263biological_processGMP salvage
B0032264biological_processIMP salvage
B0034774cellular_componentsecretory granule lumen
B0044209biological_processAMP salvage
B0046083biological_processadenine metabolic process
B0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues19
Detailsbinding site for residue AMP A 200
ChainResidue
AVAL25
AGLY133
AGLY134
ATHR135
ALEU159
APPV201
AHOH301
AHOH311
AHOH312
AHOH340
AHOH349
APHE26
AARG27
AARG67
AASP127
AASP128
ALEU129
AALA131
ATHR132

site_idAC2
Number of Residues6
Detailsbinding site for residue PPV A 201
ChainResidue
ASER66
AARG67
AAMP200
AHOH315
BARG87
BLYS91

site_idAC3
Number of Residues20
Detailsbinding site for residue AMP B 201
ChainResidue
BVAL25
BPHE26
BARG27
BARG67
BASP127
BASP128
BLEU129
BALA131
BTHR132
BGLY133
BGLY134
BTHR135
BLEU159
BMG202
BPPV203
BHOH323
BHOH333
BHOH336
BHOH340
BHOH343

site_idAC4
Number of Residues4
Detailsbinding site for residue MG B 202
ChainResidue
BAMP201
BPPV203
BHOH304
BHOH333

site_idAC5
Number of Residues11
Detailsbinding site for residue PPV B 203
ChainResidue
AARG87
ALYS91
BSER66
BARG67
BLYS88
BAMP201
BMG202
BHOH303
BHOH304
BHOH333
BHOH344

Functional Information from PROSITE/UniProt
site_idPS00103
Number of Residues13
DetailsPUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. VVVVDDLLATGgT
ChainResidueDetails
AVAL123-THR135

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195
ChainResidueDetails
ASER4
BSER4

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER15
BSER15

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER30
BSER30

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19369195
ChainResidueDetails
ATYR60
BTYR60

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER66
BSER66

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS114
BLYS114

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19369195
ChainResidueDetails
ATHR135
BTHR135

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon