2HXU
Crystal structure of K220A mutant of L-Fuconate Dehydratase from Xanthomonas campestris liganded with Mg++ and L-fuconate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0016052 | biological_process | carbohydrate catabolic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016836 | molecular_function | hydro-lyase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050023 | molecular_function | L-fuconate dehydratase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 601 |
| Chain | Residue |
| A | ASP248 |
| A | GLU274 |
| A | GLU301 |
| A | LFC501 |
| A | HOH959 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 602 |
| Chain | Residue |
| A | ARG2 |
| A | ALA44 |
| A | LEU47 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 603 |
| Chain | Residue |
| A | PRO141 |
| A | GLU142 |
| A | ARG167 |
| A | THR140 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 604 |
| Chain | Residue |
| A | HIS386 |
| A | LEU387 |
| A | GLN389 |
| A | HOH781 |
| A | HOH798 |
| A | HOH879 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE LFC A 501 |
| Chain | Residue |
| A | GLY22 |
| A | ASP24 |
| A | TYR32 |
| A | TRP194 |
| A | LYS218 |
| A | ASP248 |
| A | ASN250 |
| A | GLU274 |
| A | GLU301 |
| A | HIS351 |
| A | GLY353 |
| A | GLU382 |
| A | MG601 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"17144652","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17144652","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17144652","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2004","submissionDatabase":"PDB data bank","title":"Crystal structure of L-fuconate dehydratase from Xanthomonas campestris pv. campestris str. ATCC 33913.","authors":["Fedorov A.A.","Fedorov E.V.","Yew W.S.","Gerlt J.A.","Almo S.C."]}}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 961 |
| Chain | Residue | Details |
| A | ALA220 | proton acceptor, proton donor |
| A | ASP248 | modifies pKa |
| A | GLU274 | metal ligand |
| A | GLU301 | metal ligand |
| A | ASP324 | metal ligand |
| A | HIS351 | proton acceptor, proton donor |
