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3E04

Crystal structure of human fumarate hydratase

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004333molecular_functionfumarate hydratase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005694cellular_componentchromosome
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0005829cellular_componentcytosol
A0006099biological_processtricarboxylic acid cycle
A0006106biological_processfumarate metabolic process
A0006108biological_processmalate metabolic process
A0006281biological_processDNA repair
A0006974biological_processDNA damage response
A0016829molecular_functionlyase activity
A0045239cellular_componenttricarboxylic acid cycle heteromeric enzyme complex
A0048873biological_processhomeostasis of number of cells within a tissue
A0070062cellular_componentextracellular exosome
A0120162biological_processpositive regulation of cold-induced thermogenesis
B0003824molecular_functioncatalytic activity
B0004333molecular_functionfumarate hydratase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005694cellular_componentchromosome
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0005829cellular_componentcytosol
B0006099biological_processtricarboxylic acid cycle
B0006106biological_processfumarate metabolic process
B0006108biological_processmalate metabolic process
B0006281biological_processDNA repair
B0006974biological_processDNA damage response
B0016829molecular_functionlyase activity
B0045239cellular_componenttricarboxylic acid cycle heteromeric enzyme complex
B0048873biological_processhomeostasis of number of cells within a tissue
B0070062cellular_componentextracellular exosome
B0120162biological_processpositive regulation of cold-induced thermogenesis
C0003824molecular_functioncatalytic activity
C0004333molecular_functionfumarate hydratase activity
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005694cellular_componentchromosome
C0005737cellular_componentcytoplasm
C0005739cellular_componentmitochondrion
C0005759cellular_componentmitochondrial matrix
C0005829cellular_componentcytosol
C0006099biological_processtricarboxylic acid cycle
C0006106biological_processfumarate metabolic process
C0006108biological_processmalate metabolic process
C0006281biological_processDNA repair
C0006974biological_processDNA damage response
C0016829molecular_functionlyase activity
C0045239cellular_componenttricarboxylic acid cycle heteromeric enzyme complex
C0048873biological_processhomeostasis of number of cells within a tissue
C0070062cellular_componentextracellular exosome
C0120162biological_processpositive regulation of cold-induced thermogenesis
D0003824molecular_functioncatalytic activity
D0004333molecular_functionfumarate hydratase activity
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005694cellular_componentchromosome
D0005737cellular_componentcytoplasm
D0005739cellular_componentmitochondrion
D0005759cellular_componentmitochondrial matrix
D0005829cellular_componentcytosol
D0006099biological_processtricarboxylic acid cycle
D0006106biological_processfumarate metabolic process
D0006108biological_processmalate metabolic process
D0006281biological_processDNA repair
D0006974biological_processDNA damage response
D0016829molecular_functionlyase activity
D0045239cellular_componenttricarboxylic acid cycle heteromeric enzyme complex
D0048873biological_processhomeostasis of number of cells within a tissue
D0070062cellular_componentextracellular exosome
D0120162biological_processpositive regulation of cold-induced thermogenesis
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 1
ChainResidue
ASER222
AALA226
ATHR243
AGLY245
AGLN246

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 511
ChainResidue
BARG421
BASP425
ALYS80
AILE81
AGLY82
AGLY83

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO B 1
ChainResidue
AASN188
AHOH566
BGLY364
BMET368
BLYS371
BASN373
DTHR234
DHIS235

Functional Information from PROSITE/UniProt
site_idPS00163
Number of Residues10
DetailsFUMARATE_LYASES Fumarate lyases signature. GSsiMpGKvN
ChainResidueDetails
AGLY364-ASN373

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P05042
ChainResidueDetails
AHIS235
BHIS235
CHIS235
DHIS235

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P9WN93
ChainResidueDetails
ASER365
BSER365
CSER365
DSER365

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P05042
ChainResidueDetails
ASER145
ASER186
BSER145
BSER186
CSER145
CSER186
DSER145
DSER186

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: in site B => ECO:0000250|UniProtKB:P05042
ChainResidueDetails
AHIS176
BHIS176
CHIS176
DHIS176

site_idSWS_FT_FI5
Number of Residues12
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P9WN93
ChainResidueDetails
ATHR234
DTHR234
DSER366
DLYS371
ASER366
ALYS371
BTHR234
BSER366
BLYS371
CTHR234
CSER366
CLYS371

site_idSWS_FT_FI6
Number of Residues4
DetailsSITE: Important for catalytic activity => ECO:0000250|UniProtKB:P05042
ChainResidueDetails
AGLU378
BGLU378
CGLU378
DGLU378

site_idSWS_FT_FI7
Number of Residues28
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P97807
ChainResidueDetails
ALYS61
BLYS80
BLYS115
BLYS122
BLYS223
BLYS292
CLYS61
CLYS66
CLYS80
CLYS115
CLYS122
ALYS66
CLYS223
CLYS292
DLYS61
DLYS66
DLYS80
DLYS115
DLYS122
DLYS223
DLYS292
ALYS80
ALYS115
ALYS122
ALYS223
ALYS292
BLYS61
BLYS66

site_idSWS_FT_FI8
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P97807
ChainResidueDetails
ATHR85
BTHR85
CTHR85
DTHR85

site_idSWS_FT_FI9
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR90
BTHR90
CTHR90
DTHR90

site_idSWS_FT_FI10
Number of Residues8
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS94
ALYS256
BLYS94
BLYS256
CLYS94
CLYS256
DLYS94
DLYS256

site_idSWS_FT_FI11
Number of Residues8
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P97807
ChainResidueDetails
ALYS213
ALYS502
BLYS213
BLYS502
CLYS213
CLYS502
DLYS213
DLYS502

site_idSWS_FT_FI12
Number of Residues4
DetailsMOD_RES: Phosphothreonine; by PRKDC => ECO:0000269|PubMed:26237645
ChainResidueDetails
ATHR236
BTHR236
CTHR236
DTHR236

site_idSWS_FT_FI13
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER366
BSER366
CSER366
DSER366

site_idSWS_FT_FI14
Number of Residues8
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P97807
ChainResidueDetails
ALYS467
ALYS473
BLYS467
BLYS473
CLYS467
CLYS473
DLYS467
DLYS473

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PDB entries from 2024-04-24

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