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4GA4

Crystal structure of AMP phosphorylase N-terminal deletion mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0004645molecular_function1,4-alpha-oligoglucan phosphorylase activity
A0006206biological_processpyrimidine nucleobase metabolic process
A0006213biological_processpyrimidine nucleoside metabolic process
A0016757molecular_functionglycosyltransferase activity
A0016763molecular_functionpentosyltransferase activity
A0046125biological_processpyrimidine deoxyribonucleoside metabolic process
B0004645molecular_function1,4-alpha-oligoglucan phosphorylase activity
B0006206biological_processpyrimidine nucleobase metabolic process
B0006213biological_processpyrimidine nucleoside metabolic process
B0016757molecular_functionglycosyltransferase activity
B0016763molecular_functionpentosyltransferase activity
B0046125biological_processpyrimidine deoxyribonucleoside metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 A 601
ChainResidue
AHIS164
ASER165
AASN175
ASER193

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 B 601
ChainResidue
BHIS164
BSER165
BASN175

Functional Information from PROSITE/UniProt
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

250359

PDB entries from 2026-03-11

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