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8SBS

Fumarate C - R126A in (3-(N-morpholino)propanesulfonic acid) at pH 7.5

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
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 Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000269|PubMed:9098893
ChainResidueDetails
AHIS188

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00743
ChainResidueDetails
ASER318

site_idSWS_FT_FI3
Number of Residues1
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

site_idSWS_FT_FI4
Number of Residues1
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
AALA126

site_idSWS_FT_FI5
Number of Residues1
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

site_idSWS_FT_FI6
Number of Residues1
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

site_idSWS_FT_FI7
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00743
ChainResidueDetails
ATHR187
ASER319
ALYS324

site_idSWS_FT_FI8
Number of Residues1
DetailsSITE: Important for catalytic activity => ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000305|PubMed:8909293
ChainResidueDetails
AGLU331

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

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PDB entries from 2024-11-06

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