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6UQ8

Crystal structure of R421A variant of cytosolic fumarate hydratase from Leishmania major in a complex with S-malate and malonate

Functional Information from GO Data
ChainGOidnamespacecontents
A0004333molecular_functionfumarate hydratase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006091biological_processgeneration of precursor metabolites and energy
A0006099biological_processtricarboxylic acid cycle
A0006106biological_processfumarate metabolic process
A0006108biological_processmalate metabolic process
A0016829molecular_functionlyase activity
A0016836molecular_functionhydro-lyase activity
A0020015cellular_componentglycosome
A0042803molecular_functionprotein homodimerization activity
A0051539molecular_function4 iron, 4 sulfur cluster binding
A0097014cellular_componentciliary plasm
B0004333molecular_functionfumarate hydratase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006091biological_processgeneration of precursor metabolites and energy
B0006099biological_processtricarboxylic acid cycle
B0006106biological_processfumarate metabolic process
B0006108biological_processmalate metabolic process
B0016829molecular_functionlyase activity
B0016836molecular_functionhydro-lyase activity
B0020015cellular_componentglycosome
B0042803molecular_functionprotein homodimerization activity
B0051539molecular_function4 iron, 4 sulfur cluster binding
B0097014cellular_componentciliary plasm
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue SF4 A 601
ChainResidue
ACYS133
AGLN134
AGLY214
ACYS252
ACYS346
AALA348
ALYS491
ALMR602

site_idAC2
Number of Residues12
Detailsbinding site for residue LMR A 602
ChainResidue
AASP135
AARG173
AGLY216
ATHR467
ATHR468
AARG471
ALYS491
ASF4601
AGOL606
AHOH927
BHIS334
AGLN134

site_idAC3
Number of Residues7
Detailsbinding site for residue MLA A 603
ChainResidue
AILE140
ALEU142
AGLN195
AASP197
ALYS271
ALYS274
BGLU267

site_idAC4
Number of Residues11
Detailsbinding site for residue MLA A 604
ChainResidue
APRO40
AHIS41
AHIS42
APHE47
ALYS144
AGLU207
APHE208
ALEU353
AALA354
AHIS355
AHOH711

site_idAC5
Number of Residues5
Detailsbinding site for residue GOL A 605
ChainResidue
ATYR224
AGLN225
AHOH788
AHOH833
BTYR222

site_idAC6
Number of Residues9
Detailsbinding site for residue GOL A 606
ChainResidue
AARG173
AALA421
AASP422
ATHR467
AARG471
ALMR602
AHOH746
AHOH769
AHOH837

site_idAC7
Number of Residues8
Detailsbinding site for residue GOL A 607
ChainResidue
AASN219
ALYS220
ATYR222
AARG471
AHOH816
AHOH851
AHOH954
AHOH981

site_idAC8
Number of Residues8
Detailsbinding site for residue SF4 B 601
ChainResidue
BCYS133
BGLN134
BGLY214
BCYS252
BCYS346
BALA348
BLYS491
BLMR602

site_idAC9
Number of Residues13
Detailsbinding site for residue LMR B 602
ChainResidue
AHIS334
BGLN134
BASP135
BARG173
BGLY215
BGLY216
BTHR467
BTHR468
BARG471
BLYS491
BSF4601
BHOH780
BHOH926

site_idAD1
Number of Residues6
Detailsbinding site for residue MLA B 603
ChainResidue
AGLU267
BILE140
BLEU142
BGLN195
BASP197
BLYS274

site_idAD2
Number of Residues12
Detailsbinding site for residue MLA B 604
ChainResidue
BPRO40
BHIS41
BHIS42
BPHE47
BLYS144
BGLU207
BPHE208
BTYR280
BLEU353
BALA354
BHIS355
BHOH715

site_idAD3
Number of Residues6
Detailsbinding site for residue GOL B 605
ChainResidue
ATYR222
AHOH816
BTYR224
BGLN225
BHOH749
BHOH750

site_idAD4
Number of Residues6
Detailsbinding site for residue GOL B 606
ChainResidue
BGLY470
BARG471
BASP473
BSER474
BHOH711
BHOH910

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues36
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"27528683","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5L2R","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

251422

PDB entries from 2026-04-01

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