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1FUO

FUMARASE C WITH BOUND CITRATE

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
A0006979biological_processresponse to oxidative stress
A0016829molecular_functionlyase activity
A0042802molecular_functionidentical protein binding
B0003824molecular_functioncatalytic activity
B0004333molecular_functionfumarate hydratase activity
B0005737cellular_componentcytoplasm
B0006099biological_processtricarboxylic acid cycle
B0006106biological_processfumarate metabolic process
B0006108biological_processmalate metabolic process
B0006979biological_processresponse to oxidative stress
B0016829molecular_functionlyase activity
B0042802molecular_functionidentical protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MLT A 468
ChainResidue
AARG126
AHIS129
APRO130
AASN131
AASP132

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MLT B 468
ChainResidue
BASP132
BARG126
BHIS129
BPRO130
BASN131

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE CIT A 469
ChainResidue
ATHR100
ASER139
ASER140
AASN141
ALYS324
AASN326
AHOH506
AHOH666
AHOH684
BTHR187
BHIS188

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE CIT B 469
ChainResidue
ATHR187
AHIS188
BTHR100
BSER139
BSER140
BASN141
BLYS324
BASN326
BHOH482

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 Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000269|PubMed:9098893
ChainResidueDetails
AHIS188
BHIS188

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00743
ChainResidueDetails
ASER318
BSER318

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000305|PubMed:12021453, ECO:0000305|PubMed:8909293, ECO:0000305|PubMed:9098893, ECO:0007744|PDB:1FUO, ECO:0007744|PDB:1FUP, ECO:0007744|PDB:1FUQ, ECO:0007744|PDB:1KQ7, ECO:0007744|PDB:2FUS
ChainResidueDetails
ASER98
BSER98

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:8909293, ECO:0000269|PubMed:9098893, ECO:0007744|PDB:1FUO, ECO:0007744|PDB:1FUP, ECO:0007744|PDB:1FUQ, ECO:0007744|PDB:1FUR
ChainResidueDetails
AARG126
BARG126

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: in site B => ECO:0000269|PubMed:12021453, ECO:0000269|PubMed:8909293, ECO:0000269|PubMed:9098893, ECO:0007744|PDB:1FUO, ECO:0007744|PDB:1FUP, ECO:0007744|PDB:1FUQ, ECO:0007744|PDB:1FUR, ECO:0007744|PDB:1KQ7
ChainResidueDetails
AHIS129
BHIS129

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000269|PubMed:12021453, ECO:0000269|PubMed:8909293, ECO:0000269|PubMed:9098893, ECO:0007744|PDB:1FUO, ECO:0007744|PDB:1FUP, ECO:0007744|PDB:1FUQ, ECO:0007744|PDB:1KQ7, ECO:0007744|PDB:2FUS
ChainResidueDetails
ASER139
BSER139

site_idSWS_FT_FI7
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00743
ChainResidueDetails
ATHR187
ASER319
ALYS324
BTHR187
BSER319
BLYS324

site_idSWS_FT_FI8
Number of Residues2
DetailsSITE: Important for catalytic activity => ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000305|PubMed:8909293
ChainResidueDetails
AGLU331
BGLU331

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1auw
ChainResidueDetails
ATHR187
AHIS188
BGLU331
BLYS324

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1auw
ChainResidueDetails
AGLU331
ASER318
ALYS324
BTHR187
BHIS188

site_idMCSA1
Number of Residues4
DetailsM-CSA 569
ChainResidueDetails
AHIS188electrostatic stabiliser, proton acceptor
ASER318proton donor
ALYS324electrostatic stabiliser
AGLU331increase basicity

site_idMCSA2
Number of Residues4
DetailsM-CSA 569
ChainResidueDetails
BHIS188electrostatic stabiliser, proton acceptor
BSER318proton donor
BLYS324electrostatic stabiliser
BGLU331increase basicity

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PDB entries from 2024-11-06

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