2FUA
L-FUCULOSE 1-PHOSPHATE ALDOLASE CRYSTAL FORM T WITH COBALT
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005829 | cellular_component | cytosol |
| A | 0005996 | biological_process | monosaccharide metabolic process |
| A | 0006004 | biological_process | fucose metabolic process |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0008738 | molecular_function | L-fuculose-phosphate aldolase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016830 | molecular_function | carbon-carbon lyase activity |
| A | 0016832 | molecular_function | aldehyde-lyase activity |
| A | 0019317 | biological_process | fucose catabolic process |
| A | 0019323 | biological_process | pentose catabolic process |
| A | 0019568 | biological_process | arabinose catabolic process |
| A | 0019571 | biological_process | D-arabinose catabolic process |
| A | 0042355 | biological_process | L-fucose catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CO A 216 |
| Chain | Residue |
| A | GLU73 |
| A | HIS92 |
| A | HIS94 |
| A | TYR113 |
| A | HIS155 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 300 |
| Chain | Residue |
| A | ASN29 |
| A | THR43 |
| A | SER71 |
| A | SER72 |
| A | HOH401 |
| A | HOH417 |
| A | HOH444 |
| A | HOH449 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 A 301 |
| Chain | Residue |
| A | HIS64 |
| A | GLU66 |
| A | GLY67 |
| A | TRP74 |
| A | ARG75 |
| A | TYR209 |
| A | HOH476 |
| A | HOH478 |
| A | HOH503 |
| A | HOH506 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BME A 302 |
| Chain | Residue |
| A | CYS14 |
| A | GLY28 |
| A | ILE45 |
| A | HOH417 |
| site_id | ACT |
| Number of Residues | 5 |
| Details | THE ACTIVE SITE IS DEFINED BY THE COBALT ION AND THE FOUR COBALT COORDINATING RESIDUES. |
| Chain | Residue |
| A | CO216 |
| A | GLU73 |
| A | HIS92 |
| A | HIS94 |
| A | HIS155 |
| site_id | PBS |
| Number of Residues | 5 |
| Details | THE PHOSPHATE BINDING SITE NEAR THE ACTIVE CENTER IS OCCUPIED BY A SULFATE ION FROM THE SOLVENT (SO4 300); FIVE RESIDUES ARE INVOLVED IN BINDING OF THE SULFATE. |
| Chain | Residue |
| A | GLY44 |
| A | SER71 |
| A | SER72 |
| A | ASN29 |
| A | THR43 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:10821675, ECO:0000269|PubMed:11054289 |
| Chain | Residue | Details |
| A | GLU73 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11054289, ECO:0000269|PubMed:8676381, ECO:0007744|PDB:1E47, ECO:0007744|PDB:1E48, ECO:0007744|PDB:4FUA |
| Chain | Residue | Details |
| A | GLY28 | |
| A | THR43 | |
| A | SER71 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00987, ECO:0000269|PubMed:10821675, ECO:0000269|PubMed:11054289, ECO:0000269|PubMed:15299567, ECO:0000269|PubMed:8676381, ECO:0007744|PDB:1DZU, ECO:0007744|PDB:1DZV, ECO:0007744|PDB:1DZW, ECO:0007744|PDB:1DZX, ECO:0007744|PDB:1DZY, ECO:0007744|PDB:1DZZ, ECO:0007744|PDB:1E48, ECO:0007744|PDB:1E49, ECO:0007744|PDB:1E4A, ECO:0007744|PDB:1E4B, ECO:0007744|PDB:1E4C, ECO:0007744|PDB:1FUA, ECO:0007744|PDB:2FUA, ECO:0007744|PDB:3FUA, ECO:0007744|PDB:4FUA |
| Chain | Residue | Details |
| A | GLU73 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00987, ECO:0000269|PubMed:10821675, ECO:0000269|PubMed:11054289, ECO:0000269|PubMed:15299567, ECO:0000269|PubMed:8676381, ECO:0007744|PDB:1DZU, ECO:0007744|PDB:1DZV, ECO:0007744|PDB:1DZW, ECO:0007744|PDB:1DZX, ECO:0007744|PDB:1DZY, ECO:0007744|PDB:1DZZ, ECO:0007744|PDB:1E46, ECO:0007744|PDB:1E47, ECO:0007744|PDB:1E48, ECO:0007744|PDB:1E49, ECO:0007744|PDB:1E4A, ECO:0007744|PDB:1E4B, ECO:0007744|PDB:1E4C, ECO:0007744|PDB:1FUA, ECO:0007744|PDB:2FUA, ECO:0007744|PDB:3FUA, ECO:0007744|PDB:4FUA |
| Chain | Residue | Details |
| A | HIS92 | |
| A | HIS94 | |
| A | HIS155 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | SITE: Plays a key role in the stabilization of the transition state and positioning the aldehyde component => ECO:0000269|PubMed:10821675 |
| Chain | Residue | Details |
| A | TYR113 | |
| A | PHE131 | |
| A | TYR209 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1fua |
| Chain | Residue | Details |
| A | TYR113 | |
| A | GLU73 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1fua |
| Chain | Residue | Details |
| A | ALA117 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 72 |
| Chain | Residue | Details |
| A | GLU73 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | HIS92 | metal ligand |
| A | HIS94 | metal ligand |
| A | TYR113 | electrostatic stabiliser, transition state stabiliser |
| A | HIS155 | metal ligand |
| A | TYR209 | electrostatic stabiliser, transition state stabiliser |
