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6UQM

Crystal structure of R173A variant of cytosolic fumarate hydratase from Leishmania major in a complex with S-malate

Functional Information from GO Data
ChainGOidnamespacecontents
A0004333molecular_functionfumarate hydratase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006091biological_processgeneration of precursor metabolites and energy
A0006106biological_processfumarate metabolic process
A0006108biological_processmalate metabolic process
A0016829molecular_functionlyase activity
A0016836molecular_functionhydro-lyase activity
A0020015cellular_componentglycosome
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
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
B0006106biological_processfumarate metabolic process
B0006108biological_processmalate metabolic process
B0016829molecular_functionlyase activity
B0016836molecular_functionhydro-lyase activity
B0020015cellular_componentglycosome
B0042803molecular_functionprotein homodimerization activity
B0046872molecular_functionmetal ion binding
B0051539molecular_function4 iron, 4 sulfur cluster binding
B0097014cellular_componentciliary plasm
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue SF4 A 601
ChainResidue
ACYS133
ALMR602
AGLN134
AASP135
AGLY214
AGLY216
ACYS252
ACYS346
AALA348
ALYS491

site_idAC2
Number of Residues12
Detailsbinding site for residue LMR A 602
ChainResidue
AGLN134
AASP135
AGLY216
APRO466
ATHR467
ATHR468
AARG471
ALYS491
ASF4601
AHOH704
AHOH724
BALA336

site_idAC3
Number of Residues5
Detailsbinding site for residue GOL A 603
ChainResidue
ATYR224
AGLN225
AHOH725
AHOH918
BTYR222

site_idAC4
Number of Residues9
Detailsbinding site for residue GOL A 604
ChainResidue
ATYR174
AASN187
AARG421
AMET538
AGLU539
AHOH724
BHIS334
BGLY335
BALA336

site_idAC5
Number of Residues6
Detailsbinding site for residue GOL A 605
ChainResidue
AASN219
ALYS220
ATYR222
AARG471
AHOH718
BGLN225

site_idAC6
Number of Residues9
Detailsbinding site for residue SF4 B 601
ChainResidue
BCYS133
BGLN134
BGLY214
BGLY216
BCYS252
BCYS346
BALA348
BLYS491
BLMR602

site_idAC7
Number of Residues13
Detailsbinding site for residue LMR B 602
ChainResidue
AALA336
BGLN134
BASP135
BGLY215
BGLY216
BARG421
BPRO466
BTHR467
BTHR468
BARG471
BLYS491
BSF4601
BHOH857

site_idAC8
Number of Residues4
Detailsbinding site for residue GOL B 603
ChainResidue
BLYS55
BTYR56
BLYS69
BHOH706

site_idAC9
Number of Residues9
Detailsbinding site for residue GOL B 604
ChainResidue
AGLY335
BTHR177
BASN187
BILE423
BLEU536
BMET538
BGLU539
BHOH750
BHOH868

site_idAD1
Number of Residues7
Detailsbinding site for residue GOL B 605
ChainResidue
APHE35
AHOH978
BALA194
BGLN195
BLEU196
BASP197
BHOH1009

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsBINDING: BINDING => ECO:0000269|PubMed:27528683, ECO:0007744|PDB:5L2R
ChainResidueDetails
ACYS133
ALYS491
BCYS133
BGLN134
BALA173
BGLY216
BASN219
BCYS252
BCYS346
BARG421
BTHR467
AGLN134
BLYS491
AALA173
AGLY216
AASN219
ACYS252
ACYS346
AARG421
ATHR467

223790

PDB entries from 2024-08-14

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