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9PDH

X-ray structure of WT Drosophila Ahcy bound to NAD and adenosine at 2.50 A

Functional Information from GO Data
ChainGOidnamespacecontents
A0004013molecular_functionadenosylhomocysteinase activity
A0005829cellular_componentcytosol
A0006730biological_processone-carbon metabolic process
A0016787molecular_functionhydrolase activity
A0033353biological_processS-adenosylmethionine cycle
B0004013molecular_functionadenosylhomocysteinase activity
B0005829cellular_componentcytosol
B0006730biological_processone-carbon metabolic process
B0016787molecular_functionhydrolase activity
B0033353biological_processS-adenosylmethionine cycle
C0004013molecular_functionadenosylhomocysteinase activity
C0005829cellular_componentcytosol
C0006730biological_processone-carbon metabolic process
C0016787molecular_functionhydrolase activity
C0033353biological_processS-adenosylmethionine cycle
D0004013molecular_functionadenosylhomocysteinase activity
D0005829cellular_componentcytosol
D0006730biological_processone-carbon metabolic process
D0016787molecular_functionhydrolase activity
D0033353biological_processS-adenosylmethionine cycle
Functional Information from PROSITE/UniProt
site_idPS00738
Number of Residues15
DetailsADOHCYASE_1 S-adenosyl-L-homocysteine hydrolase signature 1. SCNiFSTQDnAAAAI
ChainResidueDetails
ASER77-ILE91

site_idPS00739
Number of Residues17
DetailsADOHCYASE_2 S-adenosyl-L-homocysteine hydrolase signature 2. GKvccVaGYGdVGKGc.A
ChainResidueDetails
AGLY213-ALA229

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues96
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P10760","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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