3E04
Crystal structure of human fumarate hydratase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000050 | biological_process | urea cycle |
| 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 | 0006525 | biological_process | arginine metabolic process |
| A | 0006974 | biological_process | DNA damage response |
| 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 | 0000050 | biological_process | urea cycle |
| 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 | 0006525 | biological_process | arginine metabolic process |
| B | 0006974 | biological_process | DNA damage response |
| 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 | 0000050 | biological_process | urea cycle |
| 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 | 0006525 | biological_process | arginine metabolic process |
| C | 0006974 | biological_process | DNA damage response |
| 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 | 0000050 | biological_process | urea cycle |
| 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 | 0006525 | biological_process | arginine metabolic process |
| D | 0006974 | biological_process | DNA damage response |
| 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 | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"P05042","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P05042","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {"description":"in site B","evidences":[{"source":"UniProtKB","id":"P05042","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P9WN93","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Site: {"description":"Important for catalytic activity","evidences":[{"source":"UniProtKB","id":"P05042","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 28 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P97807","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P97807","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P97807","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphothreonine; by PRKDC","evidences":[{"source":"PubMed","id":"26237645","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 5 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P97807","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"UniProtKB","id":"P9WN93","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
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 |
