1FUR
FUMARASE MUTANT H188N WITH BOUND SUBSTRATE L-MALATE AT PUTATIVE ACTIVATOR SITE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004333 | molecular_function | fumarate hydratase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006099 | biological_process | tricarboxylic acid cycle |
| A | 0006106 | biological_process | fumarate metabolic process |
| A | 0006108 | biological_process | malate metabolic process |
| A | 0006979 | biological_process | response to oxidative stress |
| A | 0008152 | biological_process | metabolic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0045239 | cellular_component | tricarboxylic acid cycle heteromeric enzyme complex |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004333 | molecular_function | fumarate hydratase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006099 | biological_process | tricarboxylic acid cycle |
| B | 0006106 | biological_process | fumarate metabolic process |
| B | 0006108 | biological_process | malate metabolic process |
| B | 0006979 | biological_process | response to oxidative stress |
| B | 0008152 | biological_process | metabolic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0045239 | cellular_component | tricarboxylic acid cycle heteromeric enzyme complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MLT A 468 |
| Chain | Residue |
| A | ARG126 |
| A | HIS129 |
| A | PRO130 |
| A | ASN131 |
| A | ASP132 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MLT B 468 |
| Chain | Residue |
| B | ARG126 |
| B | HIS129 |
| B | PRO130 |
| B | ASN131 |
| B | ASP132 |
| B | MET124 |
| site_id | S1 |
| Number of Residues | 3 |
| Details | THE ACTIVE SITE IS GENERATED FROM THREE OF THE FOUR SUBUNITS WITHIN THE TETRAMER. THE ENTRY CONTAINS CHAINS A AND B. CHAINS C AND D CAN BE GENERATED FROM CHAINS A AND B. THE ACTIVE SITE CONTAINS RESIDUES FROM CHAINS B, C, AND D. BECAUSE OF PDB FORMAT RESTRICTIONS, ONLY THE RESIDUES FROM CHAIN B ARE LISTED ON THE SITE RECORD BELOW. THE FOLLOWING RESIDUES ARE ALSO PART OF THE ACTIVE SITE: LYS C 324 ASN C 326 GLU C 331 ASN D 188 |
| Chain | Residue |
| B | SER98 |
| B | THR100 |
| B | ASN141 |
Functional Information from PROSITE/UniProt
| site_id | PS00163 |
| Number of Residues | 10 |
| Details | FUMARATE_LYASES Fumarate lyases signature. GSsiMpGKvN |
| Chain | Residue | Details |
| A | GLY317-ASN326 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000269|PubMed:9098893 |
| Chain | Residue | Details |
| A | ASN188 | |
| B | ASN188 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00743 |
| Chain | Residue | Details |
| A | SER318 | |
| B | SER318 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000305|PubMed:12021453, ECO:0000305|PubMed:8909293, ECO:0000305|PubMed:9098893, ECO:0007744|PDB:1FUO, ECO:0007744|PDB:1FUP, ECO:0007744|PDB:1FUQ, ECO:0007744|PDB:1KQ7, ECO:0007744|PDB:2FUS |
| Chain | Residue | Details |
| A | SER98 | |
| B | SER98 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:8909293, ECO:0000269|PubMed:9098893, ECO:0007744|PDB:1FUO, ECO:0007744|PDB:1FUP, ECO:0007744|PDB:1FUQ, ECO:0007744|PDB:1FUR |
| Chain | Residue | Details |
| A | ARG126 | |
| B | ARG126 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: in site B => ECO:0000269|PubMed:12021453, ECO:0000269|PubMed:8909293, ECO:0000269|PubMed:9098893, ECO:0007744|PDB:1FUO, ECO:0007744|PDB:1FUP, ECO:0007744|PDB:1FUQ, ECO:0007744|PDB:1FUR, ECO:0007744|PDB:1KQ7 |
| Chain | Residue | Details |
| A | HIS129 | |
| B | HIS129 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000269|PubMed:12021453, ECO:0000269|PubMed:8909293, ECO:0000269|PubMed:9098893, ECO:0007744|PDB:1FUO, ECO:0007744|PDB:1FUP, ECO:0007744|PDB:1FUQ, ECO:0007744|PDB:1KQ7, ECO:0007744|PDB:2FUS |
| Chain | Residue | Details |
| A | SER139 | |
| B | SER139 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00743 |
| Chain | Residue | Details |
| A | THR187 | |
| A | SER319 | |
| A | LYS324 | |
| B | THR187 | |
| B | SER319 | |
| B | LYS324 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | SITE: Important for catalytic activity => ECO:0000255|HAMAP-Rule:MF_00743, ECO:0000305|PubMed:8909293 |
| Chain | Residue | Details |
| A | GLU331 | |
| B | GLU331 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 569 |
| Chain | Residue | Details |
| A | ASN188 | electrostatic stabiliser, proton acceptor |
| A | SER318 | proton donor |
| A | LYS324 | electrostatic stabiliser |
| A | GLU331 | increase basicity |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 569 |
| Chain | Residue | Details |
| B | ASN188 | electrostatic stabiliser, proton acceptor |
| B | SER318 | proton donor |
| B | LYS324 | electrostatic stabiliser |
| B | GLU331 | increase basicity |
