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7ZD9

Crystal structure of the E352T mutant of S-adenosyl-L-homocysteine hydrolase from Synechocystis sp. PCC 6803 cocrystallized with adenosine in the presence of Rb+ cations

Functional Information from GO Data
ChainGOidnamespacecontents
A0004013molecular_functionadenosylhomocysteinase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006730biological_processone-carbon metabolic process
A0016787molecular_functionhydrolase activity
A0033353biological_processS-adenosylmethionine cycle
C0004013molecular_functionadenosylhomocysteinase activity
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006730biological_processone-carbon metabolic process
C0016787molecular_functionhydrolase activity
C0033353biological_processS-adenosylmethionine cycle
Functional Information from PROSITE/UniProt
site_idPS00738
Number of Residues15
DetailsADOHCYASE_1 S-adenosyl-L-homocysteine hydrolase signature 1. ASNpLSTQDdVAACL
ChainResidueDetails
AALA81-LEU95

site_idPS00739
Number of Residues17
DetailsADOHCYASE_2 S-adenosyl-L-homocysteine hydrolase signature 2. GKtivVaGYGwCGKGv.A
ChainResidueDetails
AGLY214-ALA230

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00563
ChainResidueDetails
AASN192
AGLY221
AGLU244
AASN279
ASER300
AASN347
CTHR60
CASP132
CGLU157
CTHR158
CLYS187
CASP191
CASN192
CGLY221
CGLU244
CASN279
CSER300
CASN347
ATHR60
AASP132
AGLU157
ATHR158
ALYS187
AASP191

219869

PDB entries from 2024-05-15

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