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1ZN8

Human Adenine Phosphoribosyltransferase Complexed with AMP, in Space Group P1 at 1.76 A Resolution

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 Residues3
DetailsBINDING SITE FOR RESIDUE CL B 1030
ChainResidue
BTRP98
BARG145
BHOH1211

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE AMP A 1031
ChainResidue
ALEU129
AALA131
ATHR132
AGLY133
AGLY134
ATHR135
ALEU159
AHOH1032
AHOH1033
AHOH1034
AHOH1061
AHOH1093
AHOH1114
AHOH1158
AVAL25
APHE26
AARG27
AARG67
AASP127
AASP128

site_idAC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE AMP B 1032
ChainResidue
BVAL25
BPHE26
BARG27
BARG67
BASP127
BASP128
BALA131
BTHR132
BGLY133
BGLY134
BTHR135
BLEU159
BHOH1033
BHOH1034
BHOH1068
BHOH1084
BHOH1127

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: N-acetylalanine => ECO:0000269|PubMed:12665801, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712
ChainResidueDetails
AASP3
BASP3

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195
ChainResidueDetails
AGLU5
BGLU5

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163
ChainResidueDetails
APHE16
BPHE16

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
APRO31
BPRO31

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19369195
ChainResidueDetails
AILE61
BILE61

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
AARG67
BARG67

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
AASP115
BASP115

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19369195
ChainResidueDetails
AMET136
BMET136

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oro
ChainResidueDetails
ALYS91

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oro
ChainResidueDetails
BLYS91

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1oro
ChainResidueDetails
AGLU104
AARG67

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1oro
ChainResidueDetails
BGLU104
BARG67

224201

PDB entries from 2024-08-28

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