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4GA6

Crystal structure of AMP phosphorylase C-terminal deletion mutant in complex with substrates

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004645molecular_function1,4-alpha-oligoglucan phosphorylase activity
A0005829cellular_componentcytosol
A0006196biological_processAMP catabolic process
A0006206biological_processpyrimidine nucleobase metabolic process
A0006213biological_processpyrimidine nucleoside metabolic process
A0009032molecular_functionthymidine phosphorylase activity
A0016208molecular_functionAMP binding
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0016763molecular_functionpentosyltransferase activity
A0042301molecular_functionphosphate ion binding
A0046125biological_processpyrimidine deoxyribonucleoside metabolic process
B0003824molecular_functioncatalytic activity
B0004645molecular_function1,4-alpha-oligoglucan phosphorylase activity
B0005829cellular_componentcytosol
B0006196biological_processAMP catabolic process
B0006206biological_processpyrimidine nucleobase metabolic process
B0006213biological_processpyrimidine nucleoside metabolic process
B0009032molecular_functionthymidine phosphorylase activity
B0016208molecular_functionAMP binding
B0016740molecular_functiontransferase activity
B0016757molecular_functionglycosyltransferase activity
B0016763molecular_functionpentosyltransferase activity
B0042301molecular_functionphosphate ion binding
B0046125biological_processpyrimidine deoxyribonucleoside metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE AMP A 601
ChainResidue
AHIS164
ATHR203
AASP256
AMET261
ASER264
ALYS288
ASO4602
AHOH839
ASER165
AILE166
AGLY168
ASER194
AALA196
AILE197
ATHR198
ASER199

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 602
ChainResidue
AHIS164
ASER165
AASN175
ALYS191
ASER193
ATHR203
AAMP601
AHOH708
AHOH742

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 603
ChainResidue
AHIS326
APRO347
AGLY348
ASER349
ALYS455
AHOH820

site_idAC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE AMP B 601
ChainResidue
BHIS164
BSER165
BILE166
BGLY167
BGLY168
BSER193
BSER194
BALA196
BILE197
BTHR198
BSER199
BTHR203
BASP256
BMET261
BSER264
BLYS288
BSO4602
BHOH795

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 B 602
ChainResidue
BHIS164
BSER165
BASN175
BLYS191
BSER193
BTHR203
BAMP601
BHOH728
BHOH785

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 603
ChainResidue
BHIS326
BGLY348
BSER349
BLYS455
BHOH798

Functional Information from PROSITE/UniProt
site_idPS00430
Number of Residues82
DetailsTONB_DEPENDENT_REC_1 TonB-dependent receptor (TBDR) proteins signature 1. mkakirildmfsgrytvlineedakeaklhpddlvkieagkkavygsvalsnlvgkgevgisrdvldlhnfseg.........................................ETVSVIPA
ChainResidueDetails
AMET1-ALA82

site_idPS00647
Number of Residues16
DetailsTHYMID_PHOSPHORYLASE Thymidine and pyrimidine-nucleoside phosphorylases signature. SSRAItsAAGTaDvVE
ChainResidueDetails
ASER193-GLU208

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"23659790","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"23659790","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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