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5F92

Fumarate hydratase of Mycobacterium tuberculosis in complex with formate

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004333molecular_functionfumarate hydratase activity
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006099biological_processtricarboxylic acid cycle
A0006106biological_processfumarate metabolic process
A0009274cellular_componentpeptidoglycan-based cell wall
A0016829molecular_functionlyase activity
B0003824molecular_functioncatalytic activity
B0004333molecular_functionfumarate hydratase activity
B0005576cellular_componentextracellular region
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006099biological_processtricarboxylic acid cycle
B0006106biological_processfumarate metabolic process
B0009274cellular_componentpeptidoglycan-based cell wall
B0016829molecular_functionlyase activity
C0003824molecular_functioncatalytic activity
C0004333molecular_functionfumarate hydratase activity
C0005576cellular_componentextracellular region
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0006099biological_processtricarboxylic acid cycle
C0006106biological_processfumarate metabolic process
C0009274cellular_componentpeptidoglycan-based cell wall
C0016829molecular_functionlyase activity
D0003824molecular_functioncatalytic activity
D0004333molecular_functionfumarate hydratase activity
D0005576cellular_componentextracellular region
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0005886cellular_componentplasma membrane
D0006099biological_processtricarboxylic acid cycle
D0006106biological_processfumarate metabolic process
D0009274cellular_componentpeptidoglycan-based cell wall
D0016829molecular_functionlyase activity
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue FMT A 501
ChainResidue
ASER318
AMET321
ALYS324
AASN326
AFMT502
CTHR186
CHIS187
DASN140
DHOH641

site_idAC2
Number of Residues8
Detailsbinding site for residue FMT A 502
ChainResidue
ASER318
ASER319
AILE320
AFMT501
DTHR106
DSER138
DSER139
DHOH641

site_idAC3
Number of Residues1
Detailsbinding site for residue CL A 503
ChainResidue
AGLN198

site_idAC4
Number of Residues2
Detailsbinding site for residue PG4 A 504
ChainResidue
ALEU303
CLEU429

site_idAC5
Number of Residues8
Detailsbinding site for residue FMT B 501
ChainResidue
BSER318
BMET321
BLYS324
BASN326
CASN140
CHOH556
DTHR186
DHIS187

site_idAC6
Number of Residues6
Detailsbinding site for residue FMT B 502
ChainResidue
BSER318
BSER319
BILE320
CTHR106
CSER138
CSER139

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000305|PubMed:22561013, ECO:0007744|PDB:4ADL, ECO:0007744|PDB:4ADM
ChainResidueDetails
AHIS187
BHIS187
CHIS187
DHIS187

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000269|PubMed:22561013, ECO:0007744|PDB:4ADM
ChainResidueDetails
ASER318
BSER318
CSER318
DSER318

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000269|PubMed:22561013, ECO:0000269|PubMed:27325754, ECO:0007744|PDB:4ADL, ECO:0007744|PDB:4ADM, ECO:0007744|PDB:4APB, ECO:0007744|PDB:5F92
ChainResidueDetails
ASER104
BSER104
CSER104
DSER104

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: in site B => ECO:0000255|HAMAP-Rule:MF_00743
ChainResidueDetails
AHIS128
BHIS128
CHIS128
DHIS128

site_idSWS_FT_FI5
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000269|PubMed:22561013, ECO:0000269|PubMed:27325754, ECO:0007744|PDB:4ADL, ECO:0007744|PDB:4ADM, ECO:0007744|PDB:4APB, ECO:0007744|PDB:5F91, ECO:0007744|PDB:5F92
ChainResidueDetails
ASER138
ALYS324
BSER138
BLYS324
CSER138
CLYS324
DSER138
DLYS324

site_idSWS_FT_FI6
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000269|PubMed:22561013, ECO:0000269|PubMed:27325754, ECO:0007744|PDB:4ADL, ECO:0007744|PDB:4APB, ECO:0007744|PDB:5F91, ECO:0007744|PDB:5F92
ChainResidueDetails
ATHR186
BTHR186
CTHR186
DTHR186

site_idSWS_FT_FI7
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000269|PubMed:22561013, ECO:0000269|PubMed:27325754, ECO:0007744|PDB:4ADL, ECO:0007744|PDB:4APB, ECO:0007744|PDB:5F92
ChainResidueDetails
ASER319
BSER319
CSER319
DSER319

site_idSWS_FT_FI8
Number of Residues4
DetailsSITE: Important for catalytic activity => ECO:0000255|HAMAP-Rule:MF_00743
ChainResidueDetails
AGLU331
BGLU331
CGLU331
DGLU331

site_idSWS_FT_FI9
Number of Residues4
DetailsMOD_RES: N-acetylalanine => ECO:0007744|PubMed:21969609
ChainResidueDetails
AALA2
BALA2
CALA2
DALA2

222415

PDB entries from 2024-07-10

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