3RGT
Crystal structure of d-mannonate dehydratase from Chromohalobacter salexigens complexed with D-Arabinohydroxamate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0008927 | molecular_function | mannonate dehydratase activity |
| A | 0009063 | biological_process | amino acid catabolic process |
| A | 0016052 | biological_process | carbohydrate catabolic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047929 | molecular_function | gluconate dehydratase activity |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0008927 | molecular_function | mannonate dehydratase activity |
| B | 0009063 | biological_process | amino acid catabolic process |
| B | 0016052 | biological_process | carbohydrate catabolic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047929 | molecular_function | gluconate dehydratase activity |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0008927 | molecular_function | mannonate dehydratase activity |
| C | 0009063 | biological_process | amino acid catabolic process |
| C | 0016052 | biological_process | carbohydrate catabolic process |
| C | 0016829 | molecular_function | lyase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0047929 | molecular_function | gluconate dehydratase activity |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0008927 | molecular_function | mannonate dehydratase activity |
| D | 0009063 | biological_process | amino acid catabolic process |
| D | 0016052 | biological_process | carbohydrate catabolic process |
| D | 0016829 | molecular_function | lyase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0047929 | molecular_function | gluconate dehydratase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CO A 406 |
| Chain | Residue |
| A | ASP213 |
| A | GLU239 |
| A | GLU265 |
| A | EZ4407 |
| A | HOH784 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE EZ4 A 407 |
| Chain | Residue |
| A | GLU265 |
| A | ARG286 |
| A | HIS315 |
| A | PRO317 |
| A | ASP319 |
| A | GLU342 |
| A | TRP405 |
| A | CO406 |
| A | HOH413 |
| C | TRP78 |
| A | ASN39 |
| A | ASP213 |
| A | HIS215 |
| A | GLU239 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CO B 406 |
| Chain | Residue |
| B | ASP213 |
| B | GLU239 |
| B | GLU265 |
| B | ARG286 |
| B | EZ4407 |
| B | HOH783 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE EZ4 B 407 |
| Chain | Residue |
| B | ASN39 |
| B | TYR161 |
| B | ASP213 |
| B | HIS215 |
| B | GLU239 |
| B | GLU265 |
| B | ARG286 |
| B | HIS315 |
| B | PRO317 |
| B | ASP319 |
| B | GLU342 |
| B | TRP405 |
| B | CO406 |
| B | HOH408 |
| D | TYR77 |
| D | TRP78 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CO C 406 |
| Chain | Residue |
| C | ASP213 |
| C | GLU239 |
| C | GLU265 |
| C | EZ4407 |
| C | HOH782 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE EZ4 C 407 |
| Chain | Residue |
| A | TRP78 |
| C | ASN39 |
| C | ASP213 |
| C | HIS215 |
| C | GLU239 |
| C | GLU265 |
| C | ARG286 |
| C | HIS315 |
| C | PRO317 |
| C | ASP319 |
| C | GLU342 |
| C | TRP405 |
| C | CO406 |
| C | HOH412 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CO D 406 |
| Chain | Residue |
| D | ASP213 |
| D | GLU239 |
| D | GLU265 |
| D | EZ4407 |
| D | HOH781 |
| site_id | AC8 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE EZ4 D 407 |
| Chain | Residue |
| B | TRP78 |
| D | ASN39 |
| D | ASP213 |
| D | HIS215 |
| D | GLU239 |
| D | GLU265 |
| D | ARG286 |
| D | HIS315 |
| D | PRO317 |
| D | ASP319 |
| D | GLU342 |
| D | TRP405 |
| D | CO406 |
| D | HOH409 |
Functional Information from PROSITE/UniProt
| site_id | PS00908 |
| Number of Residues | 26 |
| Details | MR_MLE_1 Mandelate racemase / muconate lactonizing enzyme family signature 1. AiAAVDmALwDIkAKaagmPLyqLLG |
| Chain | Residue | Details |
| A | ALA87-GLY112 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 5 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2011","submissionDatabase":"PDB data bank","title":"Crystal structure of the mutant P317A of D-mannonate dehydratase from Chromohalobacter salexigens complexed with Mg and D-Gluconate.","authors":["Fedorov A.A.","Fedorov E.V.","Wichelecki D.","Gerlt J.A.","Almo S.C."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Site: {"description":"Important for activity and substrate specificity; Pro is observed in family members with low D-mannonate dehydratase activity"} |
| Chain | Residue | Details |
