1YEY
Crystal Structure of L-fuconate Dehydratase from Xanthomonas campestris pv. campestris str. ATCC 33913
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 |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0016052 | biological_process | carbohydrate catabolic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016836 | molecular_function | hydro-lyase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050023 | molecular_function | L-fuconate dehydratase activity |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0016052 | biological_process | carbohydrate catabolic process |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016836 | molecular_function | hydro-lyase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0050023 | molecular_function | L-fuconate dehydratase activity |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0016052 | biological_process | carbohydrate catabolic process |
| D | 0016829 | molecular_function | lyase activity |
| D | 0016836 | molecular_function | hydro-lyase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0050023 | molecular_function | L-fuconate dehydratase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 6001 |
| Chain | Residue |
| A | ASP248 |
| A | ASN250 |
| A | GLU274 |
| A | GLU301 |
| A | HOH5231 |
| A | HOH5232 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 6002 |
| Chain | Residue |
| B | GLU301 |
| B | HOH5233 |
| B | HOH5234 |
| B | LYS220 |
| B | ASP248 |
| B | GLU274 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG C 6003 |
| Chain | Residue |
| C | LYS220 |
| C | ASP248 |
| C | GLU274 |
| C | GLU301 |
| C | HOH5235 |
| C | HOH5236 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG D 6004 |
| Chain | Residue |
| D | LYS220 |
| D | ASP248 |
| D | ASN250 |
| D | GLU274 |
| D | GLU301 |
| D | HOH5237 |
| D | HOH5238 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| 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 | 4 |
| Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 40 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17144652","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| 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 | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1ec9 |
| Chain | Residue | Details |
| A | LYS218 | |
| A | LYS220 | |
| A | ASP324 | |
| A | HIS351 | |
| A | ASP378 |
| site_id | CSA10 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ec9 |
| Chain | Residue | Details |
| B | LYS218 | |
| B | LYS220 | |
| B | ASP378 |
| site_id | CSA11 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ec9 |
| Chain | Residue | Details |
| C | LYS218 | |
| C | LYS220 | |
| C | ASP378 |
| site_id | CSA12 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ec9 |
| Chain | Residue | Details |
| D | LYS218 | |
| D | LYS220 | |
| D | ASP378 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1ec9 |
| Chain | Residue | Details |
| B | LYS218 | |
| B | LYS220 | |
| B | ASP324 | |
| B | HIS351 | |
| B | ASP378 |
| site_id | CSA3 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1ec9 |
| Chain | Residue | Details |
| C | LYS218 | |
| C | LYS220 | |
| C | ASP324 | |
| C | HIS351 | |
| C | ASP378 |
| site_id | CSA4 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1ec9 |
| Chain | Residue | Details |
| D | LYS218 | |
| D | LYS220 | |
| D | ASP324 | |
| D | HIS351 | |
| D | ASP378 |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1ec9 |
| Chain | Residue | Details |
| A | LYS220 | |
| A | GLU382 | |
| A | ASP324 | |
| A | HIS351 |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1ec9 |
| Chain | Residue | Details |
| B | LYS220 | |
| B | GLU382 | |
| B | ASP324 | |
| B | HIS351 |
| site_id | CSA7 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1ec9 |
| Chain | Residue | Details |
| C | LYS220 | |
| C | GLU382 | |
| C | ASP324 | |
| C | HIS351 |
| site_id | CSA8 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1ec9 |
| Chain | Residue | Details |
| D | LYS220 | |
| D | GLU382 | |
| D | ASP324 | |
| D | HIS351 |
| site_id | CSA9 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ec9 |
| Chain | Residue | Details |
| A | LYS218 | |
| A | LYS220 | |
| A | ASP378 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 961 |
| Chain | Residue | Details |
| A | ARG236 | proton acceptor, proton donor |
| A | PHE268 | modifies pKa |
| A | SER298 | metal ligand |
| A | ALA325 | metal ligand |
| A | VAL348 | metal ligand |
| A | LYS375 | proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 961 |
| Chain | Residue | Details |
| B | ARG236 | proton acceptor, proton donor |
| B | PHE268 | modifies pKa |
| B | SER298 | metal ligand |
| B | ALA325 | metal ligand |
| B | VAL348 | metal ligand |
| B | LYS375 | proton acceptor, proton donor |
| site_id | MCSA3 |
| Number of Residues | 6 |
| Details | M-CSA 961 |
| Chain | Residue | Details |
| C | ARG236 | proton acceptor, proton donor |
| C | PHE268 | modifies pKa |
| C | SER298 | metal ligand |
| C | ALA325 | metal ligand |
| C | VAL348 | metal ligand |
| C | LYS375 | proton acceptor, proton donor |
| site_id | MCSA4 |
| Number of Residues | 6 |
| Details | M-CSA 961 |
| Chain | Residue | Details |
| D | ARG236 | proton acceptor, proton donor |
| D | PHE268 | modifies pKa |
| D | SER298 | metal ligand |
| D | ALA325 | metal ligand |
| D | VAL348 | metal ligand |
| D | LYS375 | proton acceptor, proton donor |
