Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

8CFG

Crystal structure of S-adenosyl-L-homocysteine hydrolase from P. aeruginosa in complex with F2X-Entry library fragment C04

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
A0071269biological_processL-homocysteine biosynthetic process
B0004013molecular_functionadenosylhomocysteinase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006730biological_processone-carbon metabolic process
B0016787molecular_functionhydrolase activity
B0033353biological_processS-adenosylmethionine cycle
B0071269biological_processL-homocysteine biosynthetic process
C0004013molecular_functionadenosylhomocysteinase activity
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006730biological_processone-carbon metabolic process
C0016787molecular_functionhydrolase activity
C0033353biological_processS-adenosylmethionine cycle
C0071269biological_processL-homocysteine biosynthetic process
D0004013molecular_functionadenosylhomocysteinase activity
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006730biological_processone-carbon metabolic process
D0016787molecular_functionhydrolase activity
D0033353biological_processS-adenosylmethionine cycle
D0071269biological_processL-homocysteine biosynthetic process
Functional Information from PROSITE/UniProt
site_idPS00738
Number of Residues15
DetailsADOHCYASE_1 S-adenosyl-L-homocysteine hydrolase signature 1. SCNiFSTQDqAAAAI
ChainResidueDetails
ASER84-ILE98

site_idPS00739
Number of Residues17
DetailsADOHCYASE_2 S-adenosyl-L-homocysteine hydrolase signature 2. GKqalViGYGdVGKGs.S
ChainResidueDetails
AGLY221-SER237

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues72
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00563","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

238582

PDB entries from 2025-07-09

PDB statisticsPDBj update infoContact PDBjnumon