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8GST

Crystal structure of L-2,4-diketo-3-deoxyrhamnonate hydrolase from Sphingomonas sp. (pyruvate bound-form)

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0016787molecular_functionhydrolase activity
A0016853molecular_functionisomerase activity
A0019299biological_processrhamnose metabolic process
A0019752biological_processcarboxylic acid metabolic process
A0046872molecular_functionmetal ion binding
B0003824molecular_functioncatalytic activity
B0016787molecular_functionhydrolase activity
B0016853molecular_functionisomerase activity
B0019299biological_processrhamnose metabolic process
B0019752biological_processcarboxylic acid metabolic process
B0046872molecular_functionmetal ion binding
C0003824molecular_functioncatalytic activity
C0016787molecular_functionhydrolase activity
C0016853molecular_functionisomerase activity
C0019299biological_processrhamnose metabolic process
C0019752biological_processcarboxylic acid metabolic process
C0046872molecular_functionmetal ion binding
D0003824molecular_functioncatalytic activity
D0016787molecular_functionhydrolase activity
D0016853molecular_functionisomerase activity
D0019299biological_processrhamnose metabolic process
D0019752biological_processcarboxylic acid metabolic process
D0046872molecular_functionmetal ion binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:36563174, ECO:0007744|PDB:8GST
ChainResidueDetails
ALEU73
DLEU73
DLYS168
DTHR238
ALYS168
ATHR238
BLEU73
BLYS168
BTHR238
CLEU73
CLYS168
CTHR238

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:36563174, ECO:0007744|PDB:8GSR, ECO:0007744|PDB:8GST
ChainResidueDetails
AGLU119
DGLU119
DGLU121
DASP150
AGLU121
AASP150
BGLU119
BGLU121
BASP150
CGLU119
CGLU121
CASP150

238268

PDB entries from 2025-07-02

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