4FUA
L-FUCULOSE-1-PHOSPHATE ALDOLASE COMPLEX WITH PGH
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 ZN A 216 |
Chain | Residue |
A | HIS92 |
A | HIS94 |
A | TYR113 |
A | HIS155 |
A | PGH217 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 300 |
Chain | Residue |
A | ASN146 |
A | ARG147 |
A | ARG147 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE BME A 301 |
Chain | Residue |
A | CYS14 |
A | ILE45 |
A | HOH460 |
site_id | AC4 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE PGH A 217 |
Chain | Residue |
A | THR26 |
A | GLY28 |
A | ASN29 |
A | THR43 |
A | GLY44 |
A | SER71 |
A | SER72 |
A | GLU73 |
A | HIS92 |
A | HIS94 |
A | TYR113 |
A | HIS155 |
A | ZN216 |
A | HOH431 |
site_id | ACT |
Number of Residues | 6 |
Details | THE ACTIVE CENTER IS DEFINED BY THE ZINC ION, THE FOUR ZINC COORDINATING RESIDUES AND TYR-1 13 FROM THE ADJACENT SUBUNIT. |
Chain | Residue |
A | ZN216 |
A | GLU73 |
A | HIS92 |
A | HIS94 |
A | HIS155 |
A | TYR113 |
site_id | PBS |
Number of Residues | 5 |
Details | BINDING SITE FOR THE SUBSTRATE PHOSPHATE GROUP. |
Chain | Residue |
A | THR43 |
A | GLY44 |
A | SER71 |
A | SER72 |
A | ASN29 |
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 | 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 |