3P93
Crystal structure of D-mannonate dehydratase from Chromohalobacter Salexigens complexed with MG,D-Mannonate and 2-keto-3-deoxy-D-Gluconate
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 |
E | 0000287 | molecular_function | magnesium ion binding |
E | 0008927 | molecular_function | mannonate dehydratase activity |
E | 0009063 | biological_process | amino acid catabolic process |
E | 0016052 | biological_process | carbohydrate catabolic process |
E | 0016829 | molecular_function | lyase activity |
E | 0046872 | molecular_function | metal ion binding |
E | 0047929 | molecular_function | gluconate dehydratase activity |
F | 0000287 | molecular_function | magnesium ion binding |
F | 0008927 | molecular_function | mannonate dehydratase activity |
F | 0009063 | biological_process | amino acid catabolic process |
F | 0016052 | biological_process | carbohydrate catabolic process |
F | 0016829 | molecular_function | lyase activity |
F | 0046872 | molecular_function | metal ion binding |
F | 0047929 | molecular_function | gluconate dehydratase activity |
G | 0000287 | molecular_function | magnesium ion binding |
G | 0008927 | molecular_function | mannonate dehydratase activity |
G | 0009063 | biological_process | amino acid catabolic process |
G | 0016052 | biological_process | carbohydrate catabolic process |
G | 0016829 | molecular_function | lyase activity |
G | 0046872 | molecular_function | metal ion binding |
G | 0047929 | molecular_function | gluconate dehydratase activity |
H | 0000287 | molecular_function | magnesium ion binding |
H | 0008927 | molecular_function | mannonate dehydratase activity |
H | 0009063 | biological_process | amino acid catabolic process |
H | 0016052 | biological_process | carbohydrate catabolic process |
H | 0016829 | molecular_function | lyase activity |
H | 0046872 | molecular_function | metal ion binding |
H | 0047929 | molecular_function | gluconate dehydratase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 406 |
Chain | Residue |
A | ASP213 |
A | GLU239 |
A | GLU265 |
A | CS2407 |
A | HOH1933 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 406 |
Chain | Residue |
B | HOH1935 |
B | ASP213 |
B | GLU239 |
B | GLU265 |
B | CS2407 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG C 406 |
Chain | Residue |
C | ASP213 |
C | GLU239 |
C | GLU265 |
C | ARG286 |
C | KDG407 |
C | HOH408 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG D 406 |
Chain | Residue |
D | ASP213 |
D | GLU239 |
D | GLU265 |
D | KDG407 |
D | HOH1934 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG E 406 |
Chain | Residue |
E | ASP213 |
E | GLU239 |
E | GLU265 |
E | CS2407 |
E | HOH1932 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG F 406 |
Chain | Residue |
F | ASP213 |
F | GLU239 |
F | GLU265 |
F | CS2407 |
F | HOH1936 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG G 406 |
Chain | Residue |
G | ASP213 |
G | GLU239 |
G | GLU265 |
G | KDG407 |
G | HOH1931 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG H 406 |
Chain | Residue |
H | ASP213 |
H | GLU239 |
H | GLU265 |
H | KDG407 |
H | HOH1361 |
site_id | AC9 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE CS2 A 407 |
Chain | Residue |
A | ASN39 |
A | HIS124 |
A | ARG149 |
A | ASP213 |
A | HIS215 |
A | GLU239 |
A | GLU265 |
A | ARG286 |
A | HIS315 |
A | PRO317 |
A | ASP319 |
A | GLU342 |
A | TRP405 |
A | MG406 |
A | HOH442 |
H | TYR77 |
H | TRP78 |
site_id | BC1 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE CS2 B 407 |
Chain | Residue |
B | ASN39 |
B | HIS124 |
B | ARG149 |
B | ASP213 |
B | HIS215 |
B | GLU239 |
B | GLU265 |
B | ARG286 |
B | HIS315 |
B | PRO317 |
B | ASP319 |
B | GLU342 |
B | TRP405 |
B | MG406 |
B | HOH412 |
D | TYR77 |
D | TRP78 |
site_id | BC2 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE KDG C 407 |
Chain | Residue |
C | ASN39 |
C | HIS124 |
C | ARG149 |
C | ASP213 |
C | HIS215 |
C | GLU239 |
C | GLU265 |
C | ARG286 |
C | HIS315 |
C | PRO317 |
C | ASP319 |
C | GLU342 |
C | TRP405 |
C | MG406 |
C | HOH412 |
G | TYR77 |
G | TRP78 |
site_id | BC3 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE KDG D 407 |
Chain | Residue |
D | GLU265 |
D | ARG286 |
D | HIS315 |
D | PRO317 |
D | ASP319 |
D | GLU342 |
D | TRP405 |
D | MG406 |
D | HOH423 |
B | TRP78 |
D | ASN39 |
D | HIS124 |
D | ARG149 |
D | ASP213 |
D | HIS215 |
D | GLU239 |
site_id | BC4 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE CS2 E 407 |
Chain | Residue |
E | ASN39 |
E | HIS124 |
E | ARG149 |
E | ASP213 |
E | HIS215 |
E | GLU239 |
E | GLU265 |
E | ARG286 |
E | HIS315 |
E | PRO317 |
E | ASP319 |
E | GLU342 |
E | TRP405 |
E | MG406 |
E | HOH424 |
F | TYR77 |
F | TRP78 |
site_id | BC5 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE CS2 F 407 |
Chain | Residue |
E | TYR77 |
E | TRP78 |
F | ASN39 |
F | HIS124 |
F | ARG149 |
F | ASP213 |
F | HIS215 |
F | GLU239 |
F | GLU265 |
F | ARG286 |
F | HIS315 |
F | PRO317 |
F | ASP319 |
F | GLU342 |
F | TRP405 |
F | MG406 |
F | HOH430 |
site_id | BC6 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE KDG G 407 |
Chain | Residue |
C | TRP78 |
G | ASN39 |
G | HIS124 |
G | ARG149 |
G | ASP213 |
G | HIS215 |
G | GLU239 |
G | GLU265 |
G | ARG286 |
G | HIS315 |
G | PRO317 |
G | ASP319 |
G | GLU342 |
G | TRP405 |
G | MG406 |
G | HOH409 |
site_id | BC7 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE KDG H 407 |
Chain | Residue |
A | TYR77 |
A | TRP78 |
H | ASN39 |
H | HIS124 |
H | ASP213 |
H | HIS215 |
H | GLU239 |
H | GLU265 |
H | ARG286 |
H | HIS315 |
H | PRO317 |
H | ASP319 |
H | GLU342 |
H | TRP405 |
H | MG406 |
H | HOH411 |
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 | 16 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000250 |
Chain | Residue | Details |
A | TYR161 | |
E | HIS215 | |
F | TYR161 | |
F | HIS215 | |
G | TYR161 | |
G | HIS215 | |
H | TYR161 | |
H | HIS215 | |
A | HIS215 | |
B | TYR161 | |
B | HIS215 | |
C | TYR161 | |
C | HIS215 | |
D | TYR161 | |
D | HIS215 | |
E | TYR161 |
site_id | SWS_FT_FI2 |
Number of Residues | 48 |
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 | |
E | ASN39 | |
E | GLU265 | |
E | ARG286 | |
E | HIS315 | |
E | ASP319 | |
A | ARG286 | |
E | GLU342 | |
F | ASN39 | |
F | GLU265 | |
F | ARG286 | |
F | HIS315 | |
F | ASP319 | |
F | GLU342 | |
G | ASN39 | |
G | GLU265 | |
G | ARG286 | |
A | HIS315 | |
G | HIS315 | |
G | ASP319 | |
G | GLU342 | |
H | ASN39 | |
H | GLU265 | |
H | ARG286 | |
H | HIS315 | |
H | ASP319 | |
H | GLU342 | |
A | ASP319 | |
A | GLU342 | |
B | ASN39 | |
B | GLU265 | |
B | ARG286 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | HIS124 | |
B | HIS124 | |
C | HIS124 | |
D | HIS124 | |
E | HIS124 | |
F | HIS124 | |
G | HIS124 | |
H | HIS124 |
site_id | SWS_FT_FI4 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|Ref.2 |
Chain | Residue | Details |
A | ASP213 | |
E | GLU239 | |
F | ASP213 | |
F | GLU239 | |
G | ASP213 | |
G | GLU239 | |
H | ASP213 | |
H | GLU239 | |
A | GLU239 | |
B | ASP213 | |
B | GLU239 | |
C | ASP213 | |
C | GLU239 | |
D | ASP213 | |
D | GLU239 | |
E | ASP213 |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
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 | |
E | PRO317 | |
F | PRO317 | |
G | PRO317 | |
H | PRO317 |