3E04
Crystal structure of human fumarate hydratase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004333 | molecular_function | fumarate hydratase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005634 | cellular_component | nucleus |
A | 0005694 | cellular_component | chromosome |
A | 0005737 | cellular_component | cytoplasm |
A | 0005739 | cellular_component | mitochondrion |
A | 0005759 | cellular_component | mitochondrial matrix |
A | 0005829 | cellular_component | cytosol |
A | 0006099 | biological_process | tricarboxylic acid cycle |
A | 0006106 | biological_process | fumarate metabolic process |
A | 0006108 | biological_process | malate metabolic process |
A | 0006281 | biological_process | DNA repair |
A | 0016829 | molecular_function | lyase activity |
A | 0048873 | biological_process | homeostasis of number of cells within a tissue |
A | 0070062 | cellular_component | extracellular exosome |
A | 0120162 | biological_process | positive regulation of cold-induced thermogenesis |
B | 0003824 | molecular_function | catalytic activity |
B | 0004333 | molecular_function | fumarate hydratase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005634 | cellular_component | nucleus |
B | 0005694 | cellular_component | chromosome |
B | 0005737 | cellular_component | cytoplasm |
B | 0005739 | cellular_component | mitochondrion |
B | 0005759 | cellular_component | mitochondrial matrix |
B | 0005829 | cellular_component | cytosol |
B | 0006099 | biological_process | tricarboxylic acid cycle |
B | 0006106 | biological_process | fumarate metabolic process |
B | 0006108 | biological_process | malate metabolic process |
B | 0006281 | biological_process | DNA repair |
B | 0016829 | molecular_function | lyase activity |
B | 0048873 | biological_process | homeostasis of number of cells within a tissue |
B | 0070062 | cellular_component | extracellular exosome |
B | 0120162 | biological_process | positive regulation of cold-induced thermogenesis |
C | 0003824 | molecular_function | catalytic activity |
C | 0004333 | molecular_function | fumarate hydratase activity |
C | 0005515 | molecular_function | protein binding |
C | 0005634 | cellular_component | nucleus |
C | 0005694 | cellular_component | chromosome |
C | 0005737 | cellular_component | cytoplasm |
C | 0005739 | cellular_component | mitochondrion |
C | 0005759 | cellular_component | mitochondrial matrix |
C | 0005829 | cellular_component | cytosol |
C | 0006099 | biological_process | tricarboxylic acid cycle |
C | 0006106 | biological_process | fumarate metabolic process |
C | 0006108 | biological_process | malate metabolic process |
C | 0006281 | biological_process | DNA repair |
C | 0016829 | molecular_function | lyase activity |
C | 0048873 | biological_process | homeostasis of number of cells within a tissue |
C | 0070062 | cellular_component | extracellular exosome |
C | 0120162 | biological_process | positive regulation of cold-induced thermogenesis |
D | 0003824 | molecular_function | catalytic activity |
D | 0004333 | molecular_function | fumarate hydratase activity |
D | 0005515 | molecular_function | protein binding |
D | 0005634 | cellular_component | nucleus |
D | 0005694 | cellular_component | chromosome |
D | 0005737 | cellular_component | cytoplasm |
D | 0005739 | cellular_component | mitochondrion |
D | 0005759 | cellular_component | mitochondrial matrix |
D | 0005829 | cellular_component | cytosol |
D | 0006099 | biological_process | tricarboxylic acid cycle |
D | 0006106 | biological_process | fumarate metabolic process |
D | 0006108 | biological_process | malate metabolic process |
D | 0006281 | biological_process | DNA repair |
D | 0016829 | molecular_function | lyase activity |
D | 0048873 | biological_process | homeostasis of number of cells within a tissue |
D | 0070062 | cellular_component | extracellular exosome |
D | 0120162 | biological_process | positive regulation of cold-induced thermogenesis |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 1 |
Chain | Residue |
A | SER222 |
A | ALA226 |
A | THR243 |
A | GLY245 |
A | GLN246 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 511 |
Chain | Residue |
B | ARG421 |
B | ASP425 |
A | LYS80 |
A | ILE81 |
A | GLY82 |
A | GLY83 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO B 1 |
Chain | Residue |
A | ASN188 |
A | HOH566 |
B | GLY364 |
B | MET368 |
B | LYS371 |
B | ASN373 |
D | THR234 |
D | HIS235 |
Functional Information from PROSITE/UniProt
site_id | PS00163 |
Number of Residues | 10 |
Details | FUMARATE_LYASES Fumarate lyases signature. GSsiMpGKvN |
Chain | Residue | Details |
A | GLY364-ASN373 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P05042 |
Chain | Residue | Details |
A | HIS235 | |
B | HIS235 | |
C | HIS235 | |
D | HIS235 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P9WN93 |
Chain | Residue | Details |
A | SER365 | |
B | SER365 | |
C | SER365 | |
D | SER365 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P05042 |
Chain | Residue | Details |
A | SER145 | |
A | SER186 | |
B | SER145 | |
B | SER186 | |
C | SER145 | |
C | SER186 | |
D | SER145 | |
D | SER186 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: in site B => ECO:0000250|UniProtKB:P05042 |
Chain | Residue | Details |
A | HIS176 | |
B | HIS176 | |
C | HIS176 | |
D | HIS176 |
site_id | SWS_FT_FI5 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P9WN93 |
Chain | Residue | Details |
A | THR234 | |
D | THR234 | |
D | SER366 | |
D | LYS371 | |
A | SER366 | |
A | LYS371 | |
B | THR234 | |
B | SER366 | |
B | LYS371 | |
C | THR234 | |
C | SER366 | |
C | LYS371 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | SITE: Important for catalytic activity => ECO:0000250|UniProtKB:P05042 |
Chain | Residue | Details |
A | GLU378 | |
B | GLU378 | |
C | GLU378 | |
D | GLU378 |
site_id | SWS_FT_FI7 |
Number of Residues | 28 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P97807 |
Chain | Residue | Details |
A | LYS61 | |
B | LYS80 | |
B | LYS115 | |
B | LYS122 | |
B | LYS223 | |
B | LYS292 | |
C | LYS61 | |
C | LYS66 | |
C | LYS80 | |
C | LYS115 | |
C | LYS122 | |
A | LYS66 | |
C | LYS223 | |
C | LYS292 | |
D | LYS61 | |
D | LYS66 | |
D | LYS80 | |
D | LYS115 | |
D | LYS122 | |
D | LYS223 | |
D | LYS292 | |
A | LYS80 | |
A | LYS115 | |
A | LYS122 | |
A | LYS223 | |
A | LYS292 | |
B | LYS61 | |
B | LYS66 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P97807 |
Chain | Residue | Details |
A | THR85 | |
B | THR85 | |
C | THR85 | |
D | THR85 |
site_id | SWS_FT_FI9 |
Number of Residues | 4 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | THR90 | |
B | THR90 | |
C | THR90 | |
D | THR90 |
site_id | SWS_FT_FI10 |
Number of Residues | 8 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | LYS94 | |
A | LYS256 | |
B | LYS94 | |
B | LYS256 | |
C | LYS94 | |
C | LYS256 | |
D | LYS94 | |
D | LYS256 |
site_id | SWS_FT_FI11 |
Number of Residues | 8 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P97807 |
Chain | Residue | Details |
A | LYS213 | |
A | LYS502 | |
B | LYS213 | |
B | LYS502 | |
C | LYS213 | |
C | LYS502 | |
D | LYS213 | |
D | LYS502 |
site_id | SWS_FT_FI12 |
Number of Residues | 4 |
Details | MOD_RES: Phosphothreonine; by PRKDC => ECO:0000269|PubMed:26237645 |
Chain | Residue | Details |
A | THR236 | |
B | THR236 | |
C | THR236 | |
D | THR236 |
site_id | SWS_FT_FI13 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER366 | |
B | SER366 | |
C | SER366 | |
D | SER366 |
site_id | SWS_FT_FI14 |
Number of Residues | 8 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P97807 |
Chain | Residue | Details |
A | LYS467 | |
A | LYS473 | |
B | LYS467 | |
B | LYS473 | |
C | LYS467 | |
C | LYS473 | |
D | LYS467 | |
D | LYS473 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1auw |
Chain | Residue | Details |
A | LYS371 | |
A | GLU378 |
site_id | CSA10 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1auw |
Chain | Residue | Details |
C | LYS371 | |
C | GLU378 |
site_id | CSA11 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1auw |
Chain | Residue | Details |
A | HIS235 |
site_id | CSA12 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1auw |
Chain | Residue | Details |
B | HIS235 |
site_id | CSA13 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1auw |
Chain | Residue | Details |
C | HIS235 |
site_id | CSA14 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1auw |
Chain | Residue | Details |
D | HIS235 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1auw |
Chain | Residue | Details |
B | GLU378 | |
B | SER365 | |
B | LYS371 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1auw |
Chain | Residue | Details |
C | GLU378 | |
C | SER365 | |
C | LYS371 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1auw |
Chain | Residue | Details |
D | LYS371 | |
D | GLU378 |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1auw |
Chain | Residue | Details |
A | THR234 | |
A | HIS235 |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1auw |
Chain | Residue | Details |
B | THR234 | |
B | HIS235 |
site_id | CSA7 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1auw |
Chain | Residue | Details |
C | THR234 | |
C | HIS235 |
site_id | CSA8 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1auw |
Chain | Residue | Details |
D | THR234 | |
D | HIS235 |
site_id | CSA9 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1auw |
Chain | Residue | Details |
B | LYS371 | |
B | GLU378 |