2IRP
Crystal structure of the l-fuculose-1-phosphate aldolase (aq_1979) from aquifex aeolicus VF5
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0009086 | biological_process | methionine biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016830 | molecular_function | carbon-carbon lyase activity |
| A | 0019284 | biological_process | L-methionine salvage from S-adenosylmethionine |
| A | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
| A | 0046570 | molecular_function | methylthioribulose 1-phosphate dehydratase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0009086 | biological_process | methionine biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016830 | molecular_function | carbon-carbon lyase activity |
| B | 0019284 | biological_process | L-methionine salvage from S-adenosylmethionine |
| B | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
| B | 0046570 | molecular_function | methylthioribulose 1-phosphate dehydratase activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 1201 |
| Chain | Residue |
| A | LYS202 |
| A | LYS202 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL B 1202 |
| Chain | Residue |
| B | LYS202 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BME B 1101 |
| Chain | Residue |
| B | THR48 |
| B | SER50 |
| B | LEU63 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BME A 1102 |
| Chain | Residue |
| A | ARG26 |
| A | HOH1286 |
| A | HOH1373 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01677 |
| Chain | Residue | Details |
| A | HIS99 | |
| A | HIS101 | |
| B | HIS99 | |
| B | HIS101 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1fua |
| Chain | Residue | Details |
| A | GLU80 | |
| A | TYR122 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1fua |
| Chain | Residue | Details |
| B | GLU80 | |
| B | TYR122 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1fua |
| Chain | Residue | Details |
| A | LYS126 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1fua |
| Chain | Residue | Details |
| B | LYS126 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1fua |
| Chain | Residue | Details |
| A | GLU80 | |
| A | GLU123 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1fua |
| Chain | Residue | Details |
| B | GLU80 | |
| B | GLU123 |
| site_id | CSA7 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1fua |
| Chain | Residue | Details |
| A | HIS134 |
| site_id | CSA8 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1fua |
| Chain | Residue | Details |
| B | HIS134 |
