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6NZ9

Crystal structure of E. coli fumarase C bound to citrate at 1.53 angstrom resolution

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 Residues11
Detailsbinding site for residue CIT A 501
ChainResidue
ATHR100
BTHR187
BHIS188
ASER139
ASER140
AASN141
ALYS324
AASN326
AHOH604
AHOH609
AHOH627

site_idAC2
Number of Residues5
Detailsbinding site for residue CIT A 502
ChainResidue
AARG126
AHIS129
APRO130
AASN131
AASP132

site_idAC3
Number of Residues8
Detailsbinding site for residue CIT B 501
ChainResidue
BMET124
BARG126
BHIS129
BPRO130
BASN131
BASP132
BHOH624
BHOH772

site_idAC4
Number of Residues9
Detailsbinding site for residue CIT B 502
ChainResidue
ATHR187
BTHR100
BSER139
BSER140
BASN141
BLYS324
BASN326
BHOH601
BHOH604

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
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00743","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"9098893","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00743","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12021453","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"8909293","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"9098893","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1FUO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FUP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FUQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KQ7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FUS","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"8909293","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9098893","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1FUO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FUP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FUQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FUR","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {"description":"in site B","evidences":[{"source":"PubMed","id":"12021453","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8909293","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9098893","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1FUO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FUP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FUQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FUR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KQ7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00743","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12021453","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8909293","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9098893","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1FUO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FUP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1FUQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KQ7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FUS","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00743","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsSite: {"description":"Important for catalytic activity","evidences":[{"source":"HAMAP-Rule","id":"MF_00743","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"8909293","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsActive site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00743","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 569
ChainResidueDetails
AHIS188electrostatic stabiliser, proton acceptor
ALYS324electrostatic stabiliser
AGLU331increase basicity

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

246031

PDB entries from 2025-12-10

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