3OW1
Crystal structure of D-mannonate dehydratase from Chromohalobacter salexigens complexed with MG
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 | 6 |
Details | BINDING SITE FOR RESIDUE MG A 406 |
Chain | Residue |
A | ASP213 |
A | GLU239 |
A | GLU265 |
A | HOH441 |
A | HOH2093 |
A | HOH2097 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG B 406 |
Chain | Residue |
B | ARG286 |
B | HOH627 |
B | HOH2134 |
B | HOH2142 |
B | ASP213 |
B | GLU239 |
B | GLU265 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG C 406 |
Chain | Residue |
C | ASP213 |
C | GLU239 |
C | GLU265 |
C | HOH684 |
C | HOH1608 |
C | HOH2096 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG D 406 |
Chain | Residue |
D | ASP213 |
D | GLU239 |
D | GLU265 |
D | HOH2099 |
D | HOH2131 |
D | HOH2138 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG E 406 |
Chain | Residue |
E | ASP213 |
E | GLU239 |
E | GLU265 |
E | HOH2128 |
E | HOH2140 |
E | HOH2151 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG F 406 |
Chain | Residue |
F | ASP213 |
F | GLU239 |
F | GLU265 |
F | HOH1622 |
F | HOH2088 |
F | HOH2157 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG G 406 |
Chain | Residue |
G | ASP213 |
G | GLU239 |
G | GLU265 |
G | ARG286 |
G | HOH440 |
G | HOH1610 |
G | HOH2098 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG H 406 |
Chain | Residue |
H | ASP213 |
H | GLU239 |
H | GLU265 |
H | HOH2087 |
H | HOH2091 |
H | HOH2129 |
site_id | AC9 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 407 |
Chain | Residue |
A | ASN39 |
A | HIS215 |
A | HIS315 |
A | PRO317 |
A | ASP319 |
A | TRP405 |
A | HOH441 |
B | TRP78 |
site_id | BC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL B 407 |
Chain | Residue |
A | TYR77 |
A | TRP78 |
B | ASN39 |
B | HIS215 |
B | GLU265 |
B | HIS315 |
B | PRO317 |
B | ASP319 |
B | TRP405 |
B | HOH627 |
site_id | BC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL C 407 |
Chain | Residue |
C | ASN39 |
C | HIS215 |
C | HIS315 |
C | PRO317 |
C | ASP319 |
C | TRP405 |
C | HOH684 |
D | TRP78 |
site_id | BC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL D 407 |
Chain | Residue |
C | TRP78 |
D | ASN39 |
D | HIS215 |
D | HIS315 |
D | PRO317 |
D | ASP319 |
D | TRP405 |
D | HOH2138 |
site_id | BC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL E 407 |
Chain | Residue |
E | ASN39 |
E | HIS215 |
E | GLU265 |
E | HIS315 |
E | PRO317 |
E | ASP319 |
E | TRP405 |
E | HOH2151 |
F | TYR77 |
F | TRP78 |
site_id | BC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL F 407 |
Chain | Residue |
F | PRO317 |
F | ASP319 |
F | TRP405 |
F | HOH2157 |
E | TRP78 |
F | ASN39 |
F | PRO173 |
F | HIS215 |
F | HIS315 |
site_id | BC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL G 407 |
Chain | Residue |
G | ASN39 |
G | HIS215 |
G | HIS315 |
G | PRO317 |
G | ASP319 |
G | TRP405 |
G | HOH440 |
H | TYR77 |
H | TRP78 |
site_id | BC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL H 407 |
Chain | Residue |
G | TRP78 |
H | ASN39 |
H | HIS215 |
H | GLU265 |
H | HIS315 |
H | PRO317 |
H | ASP319 |
H | TRP405 |
site_id | BC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL C 408 |
Chain | Residue |
C | ALA352 |
C | LEU381 |
C | TYR385 |
C | HOH986 |
C | HOH1863 |
site_id | BC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL H 408 |
Chain | Residue |
H | ASP357 |
H | GLU369 |
H | SER370 |
H | HOH1059 |
site_id | CC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL A 408 |
Chain | Residue |
A | PRO393 |
A | SO4410 |
A | HOH1348 |
site_id | CC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 409 |
Chain | Residue |
A | THR129 |
A | ILE130 |
A | HIS192 |
A | HOH487 |
A | HOH1258 |
site_id | CC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 C 409 |
Chain | Residue |
C | THR129 |
C | ILE130 |
C | HIS192 |
C | HOH937 |
C | HOH1293 |
site_id | CC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 D 408 |
Chain | Residue |
D | THR129 |
D | ILE130 |
D | HIS192 |
D | HOH664 |
D | HOH1266 |
site_id | CC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 E 408 |
Chain | Residue |
E | THR129 |
E | ILE130 |
E | HIS192 |
E | HOH825 |
E | HOH852 |
site_id | CC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 G 408 |
Chain | Residue |
G | THR129 |
G | ILE130 |
G | HIS192 |
G | HOH1236 |
site_id | CC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 H 409 |
Chain | Residue |
H | THR129 |
H | ILE130 |
H | HIS192 |
H | HOH583 |
H | HOH1687 |
site_id | CC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 C 410 |
Chain | Residue |
C | ARG17 |
C | PRO173 |
C | THR318 |
C | HOH739 |
C | HOH767 |
C | HOH1629 |
site_id | CC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 D 409 |
Chain | Residue |
D | ARG17 |
D | PRO173 |
D | THR318 |
D | HOH477 |
D | HOH1079 |
D | HOH1662 |
site_id | DC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 G 409 |
Chain | Residue |
G | ARG17 |
G | THR318 |
G | HOH989 |
G | HOH1645 |
G | HOH1670 |
site_id | DC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 F 408 |
Chain | Residue |
F | THR129 |
F | ILE130 |
F | HIS192 |
F | HOH960 |
F | HOH1063 |
site_id | DC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 410 |
Chain | Residue |
A | ARG17 |
A | THR318 |
A | GOL408 |
A | HOH839 |
A | HOH1439 |
A | HOH1649 |
site_id | DC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 F 409 |
Chain | Residue |
F | ARG17 |
F | PRO173 |
F | THR318 |
F | HOH617 |
F | HOH1046 |
F | HOH1650 |
site_id | DC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 408 |
Chain | Residue |
B | THR129 |
B | ILE130 |
B | HIS192 |
B | HOH1047 |
B | HOH1099 |
site_id | DC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 G 410 |
Chain | Residue |
G | ARG139 |
G | HIS140 |
G | PRO345 |
G | HOH1265 |
site_id | DC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 H 410 |
Chain | Residue |
H | ARG17 |
H | PRO173 |
H | THR318 |
H | HOH543 |
H | HOH691 |
H | HOH783 |
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 | |
A | HIS215 | |
B | TYR161 | |
B | HIS215 | |
C | TYR161 | |
C | HIS215 | |
D | TYR161 | |
D | HIS215 | |
E | TYR161 | |
E | HIS215 | |
F | TYR161 | |
F | HIS215 | |
G | TYR161 | |
G | HIS215 | |
H | TYR161 | |
H | HIS215 |
site_id | SWS_FT_FI2 |
Number of Residues | 48 |
Details | BINDING: |
Chain | Residue | Details |
B | HIS315 | |
B | ASP319 | |
B | GLU342 | |
C | ASN39 | |
C | GLU265 | |
C | ARG286 | |
C | HIS315 | |
C | ASP319 | |
C | GLU342 | |
D | ASN39 | |
D | GLU265 | |
E | ASN39 | |
E | GLU265 | |
E | ARG286 | |
E | HIS315 | |
E | ASP319 | |
E | GLU342 | |
F | ASN39 | |
F | GLU265 | |
F | ARG286 | |
F | HIS315 | |
F | ASP319 | |
F | GLU342 | |
G | ASN39 | |
G | GLU265 | |
G | ARG286 | |
G | HIS315 | |
G | ASP319 | |
G | GLU342 | |
H | ASN39 | |
H | GLU265 | |
H | ARG286 | |
H | HIS315 | |
H | ASP319 | |
H | GLU342 | |
A | ASN39 | |
A | GLU265 | |
A | ARG286 | |
A | HIS315 | |
A | ASP319 | |
A | GLU342 | |
B | ASN39 | |
B | GLU265 | |
B | ARG286 | |
D | ARG286 | |
D | HIS315 | |
D | ASP319 | |
D | GLU342 |
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 |
C | GLU239 | |
E | ASP213 | |
E | GLU239 | |
F | ASP213 | |
F | GLU239 | |
G | ASP213 | |
G | GLU239 | |
H | ASP213 | |
H | GLU239 | |
A | ASP213 | |
A | GLU239 | |
B | ASP213 | |
B | GLU239 | |
C | ASP213 | |
D | ASP213 | |
D | GLU239 |
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 |