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4HGV

Crystal structure of a fumarate hydratase

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
A0016829molecular_functionlyase activity
B0003824molecular_functioncatalytic activity
B0004333molecular_functionfumarate hydratase activity
B0005737cellular_componentcytoplasm
B0006099biological_processtricarboxylic acid cycle
B0006106biological_processfumarate metabolic process
B0006108biological_processmalate metabolic process
B0016829molecular_functionlyase activity
C0003824molecular_functioncatalytic activity
C0004333molecular_functionfumarate hydratase activity
C0005737cellular_componentcytoplasm
C0006099biological_processtricarboxylic acid cycle
C0006106biological_processfumarate metabolic process
C0006108biological_processmalate metabolic process
C0016829molecular_functionlyase activity
D0003824molecular_functioncatalytic activity
D0004333molecular_functionfumarate hydratase activity
D0005737cellular_componentcytoplasm
D0006099biological_processtricarboxylic acid cycle
D0006106biological_processfumarate metabolic process
D0006108biological_processmalate metabolic process
D0016829molecular_functionlyase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 C 501
ChainResidue
ATHR197
BASN151
BHOH511
BHOH549
CLYS334
CASN336

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 D 501
ChainResidue
DSER149
DSER150
DASN113
DMSE114
DASN145

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 D 502
ChainResidue
AASN151
BTHR197
BHIS198
DLYS334
DASN336

Functional Information from PROSITE/UniProt
site_idPS00163
Number of Residues10
DetailsFUMARATE_LYASES Fumarate lyases signature. GSsiMpGKvN
ChainResidueDetails
AGLY327-ASN336

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00743
ChainResidueDetails
AHIS198
BHIS198
CHIS198
DHIS198

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00743
ChainResidueDetails
ASER328
BSER328
CSER328
DSER328

site_idSWS_FT_FI3
Number of Residues20
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00743
ChainResidueDetails
ASER108
BLYS334
CSER108
CSER149
CTHR197
CSER329
CLYS334
DSER108
DSER149
DTHR197
DSER329
ASER149
DLYS334
ATHR197
ASER329
ALYS334
BSER108
BSER149
BTHR197
BSER329

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: in site B => ECO:0000255|HAMAP-Rule:MF_00743
ChainResidueDetails
AHIS139
BHIS139
CHIS139
DHIS139

site_idSWS_FT_FI5
Number of Residues4
DetailsSITE: Important for catalytic activity => ECO:0000255|HAMAP-Rule:MF_00743
ChainResidueDetails
AGLU341
BGLU341
CGLU341
DGLU341

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PDB entries from 2024-11-06

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