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 | 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 |