3BSM
Crystal structure of D-mannonate dehydratase from Chromohalobacter salexigens
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 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 | 8 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000250 |
Chain | Residue | Details |
A | TYR161 | |
A | HIS215 | |
B | TYR161 | |
B | HIS215 | |
C | TYR161 | |
C | HIS215 | |
D | TYR161 | |
D | HIS215 |
site_id | SWS_FT_FI2 |
Number of Residues | 24 |
Details | BINDING: |
Chain | Residue | Details |
A | ASN39 | |
B | HIS315 | |
B | ASP319 | |
B | GLU342 | |
C | ASN39 | |
C | GLU265 | |
C | ARG286 | |
C | HIS315 | |
C | ASP319 | |
C | GLU342 | |
D | ASN39 | |
A | GLU265 | |
D | GLU265 | |
D | ARG286 | |
D | HIS315 | |
D | ASP319 | |
D | GLU342 | |
A | ARG286 | |
A | HIS315 | |
A | ASP319 | |
A | GLU342 | |
B | ASN39 | |
B | GLU265 | |
B | ARG286 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | HIS124 | |
B | HIS124 | |
C | HIS124 | |
D | HIS124 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|Ref.2 |
Chain | Residue | Details |
A | ASP213 | |
A | GLU239 | |
B | ASP213 | |
B | GLU239 | |
C | ASP213 | |
C | GLU239 | |
D | ASP213 | |
D | GLU239 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | SITE: Important for activity and substrate specificity; Pro is observed in family members with low D-mannonate dehydratase activity |
Chain | Residue | Details |
A | PRO317 | |
B | PRO317 | |
C | PRO317 | |
D | PRO317 |