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7MIW

Crystal Structure of Fumarate hydratase class II from Elizabethkingia anophelis NUHP1

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004333molecular_functionfumarate hydratase activity
A0005737cellular_componentcytoplasm
A0006099biological_processtricarboxylic acid cycle
A0006106biological_processfumarate metabolic process
A0006108biological_processmalate metabolic process
A0016829molecular_functionlyase activity
B0003824molecular_functioncatalytic activity
B0004333molecular_functionfumarate hydratase activity
B0005737cellular_componentcytoplasm
B0006099biological_processtricarboxylic acid cycle
B0006106biological_processfumarate metabolic process
B0006108biological_processmalate metabolic process
B0016829molecular_functionlyase activity
C0003824molecular_functioncatalytic activity
C0004333molecular_functionfumarate hydratase activity
C0005737cellular_componentcytoplasm
C0006099biological_processtricarboxylic acid cycle
C0006106biological_processfumarate metabolic process
C0006108biological_processmalate metabolic process
C0016829molecular_functionlyase activity
D0003824molecular_functioncatalytic activity
D0004333molecular_functionfumarate hydratase activity
D0005737cellular_componentcytoplasm
D0006099biological_processtricarboxylic acid cycle
D0006106biological_processfumarate metabolic process
D0006108biological_processmalate metabolic process
D0016829molecular_functionlyase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue EDO A 501
ChainResidue
ATYR356
AHOH684
AHOH690
BMET297
CTYR356
DMET297

site_idAC2
Number of Residues6
Detailsbinding site for residue EDO B 501
ChainResidue
BHOH682
CMET297
DTYR356
AMET297
BTYR356
BHOH666

Functional Information from PROSITE/UniProt
site_idPS00163
Number of Residues10
DetailsFUMARATE_LYASES Fumarate lyases signature. GSsiMpGKvN
ChainResidueDetails
AGLY317-ASN326

221051

PDB entries from 2024-06-12

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