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3RRP

Crystal structure of fumarate hydratase Fum from Mycobacterium abscessus with malate bound

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004333molecular_functionfumarate hydratase activity
A0005737cellular_componentcytoplasm
A0006099biological_processtricarboxylic acid cycle
A0006106biological_processfumarate metabolic process
A0016829molecular_functionlyase activity
B0003824molecular_functioncatalytic activity
B0004333molecular_functionfumarate hydratase activity
B0005737cellular_componentcytoplasm
B0006099biological_processtricarboxylic acid cycle
B0006106biological_processfumarate metabolic process
B0016829molecular_functionlyase activity
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE LMR A 468
ChainResidue
ASER101
BSER318
BILE319
BMET320
BLYS323
BASN325
ATHR103
ASER137
ASER138
AASN139
ATHR185
AHIS186
BGLY316
BSER317

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 469
ChainResidue
ASER403
AALA427
ALYS432
BLEU302

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE LMR B 468
ChainResidue
AGLY316
ASER317
ASER318
AILE319
AMET320
ALYS323
AASN325
BSER101
BTHR103
BSER137
BSER138
BASN139
BTHR185
BHIS186

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 469
ChainResidue
AGLU16
BGLU402
BILE407
BTHR433
BILE434
BARG435
BHOH719

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 470
ChainResidue
ALEU302
BSER403
BALA427
BLYS432
BHOH500
BHOH719

Functional Information from PROSITE/UniProt
site_idPS00163
Number of Residues10
DetailsFUMARATE_LYASES Fumarate lyases signature. GSsiMpGKvN
ChainResidueDetails
AGLY316-ASN325

221051

PDB entries from 2024-06-12

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