2QJN
Crystal structure of D-mannonate dehydratase from Novosphingobium aromaticivorans complexed with Mg 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 |
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 |
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 |
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 1001 |
Chain | Residue |
A | ASP210 |
A | GLU236 |
A | GLU262 |
A | KDG2001 |
A | HOH2154 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 1002 |
Chain | Residue |
B | HOH2173 |
B | ASP210 |
B | GLU236 |
B | GLU262 |
B | KDG2002 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG C 1003 |
Chain | Residue |
C | ASP210 |
C | GLU236 |
C | GLU262 |
C | KDG2003 |
C | HOH2157 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG D 1004 |
Chain | Residue |
D | ASP210 |
D | GLU236 |
D | GLU262 |
D | KDG2004 |
D | HOH2139 |
site_id | AC5 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE KDG A 2001 |
Chain | Residue |
A | ASN37 |
A | HIS122 |
A | ARG147 |
A | ASP210 |
A | HIS212 |
A | GLU236 |
A | GLU262 |
A | ARG283 |
A | HIS312 |
A | ALA314 |
A | ASP316 |
A | GLU339 |
A | LEU389 |
A | TRP402 |
A | MG1001 |
A | HOH2054 |
B | TRP76 |
site_id | AC6 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE KDG B 2002 |
Chain | Residue |
A | TRP76 |
B | ASN37 |
B | HIS122 |
B | ASP210 |
B | HIS212 |
B | GLU236 |
B | GLU262 |
B | ARG283 |
B | HIS312 |
B | ALA314 |
B | ASP316 |
B | GLU339 |
B | LEU389 |
B | TRP402 |
B | MG1002 |
B | HOH2028 |
site_id | AC7 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE KDG C 2003 |
Chain | Residue |
C | ASN37 |
C | HIS122 |
C | ARG147 |
C | ASP210 |
C | HIS212 |
C | GLU236 |
C | GLU262 |
C | ARG283 |
C | HIS312 |
C | ALA314 |
C | ASP316 |
C | GLU339 |
C | MET341 |
C | TRP402 |
C | MG1003 |
C | HOH2007 |
D | TRP76 |
site_id | AC8 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE KDG D 2004 |
Chain | Residue |
C | TYR75 |
C | TRP76 |
D | ASN37 |
D | ARG147 |
D | ASP210 |
D | HIS212 |
D | GLU236 |
D | GLU262 |
D | ARG283 |
D | HIS312 |
D | ALA314 |
D | ASP316 |
D | GLU339 |
D | MET341 |
D | LEU389 |
D | TRP402 |
D | MG1004 |
D | HOH2013 |
Functional Information from PROSITE/UniProt
site_id | PS00908 |
Number of Residues | 26 |
Details | MR_MLE_1 Mandelate racemase / muconate lactonizing enzyme family signature 1. AiAAVDmALwDIkAKmagmPLyqLLG |
Chain | Residue | Details |
A | ALA85-GLY110 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:17944491 |
Chain | Residue | Details |
A | TYR159 | |
A | HIS212 | |
B | TYR159 | |
B | HIS212 | |
C | TYR159 | |
C | HIS212 | |
D | TYR159 | |
D | HIS212 |
site_id | SWS_FT_FI2 |
Number of Residues | 28 |
Details | BINDING: |
Chain | Residue | Details |
A | GLU262 | |
B | ASP316 | |
B | GLU339 | |
C | ASN37 | |
C | HIS122 | |
C | GLU262 | |
C | ARG283 | |
C | HIS312 | |
C | ASP316 | |
C | GLU339 | |
D | ASN37 | |
D | HIS122 | |
D | GLU262 | |
D | ARG283 | |
D | HIS312 | |
D | ASP316 | |
D | GLU339 | |
A | ASN37 | |
A | HIS122 | |
A | ARG283 | |
A | HIS312 | |
A | ASP316 | |
A | GLU339 | |
B | ASN37 | |
B | HIS122 | |
B | GLU262 | |
B | ARG283 | |
B | HIS312 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17944491 |
Chain | Residue | Details |
A | ASP210 | |
A | GLU236 | |
B | ASP210 | |
B | GLU236 | |
C | ASP210 | |
C | GLU236 | |
D | ASP210 | |
D | GLU236 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | SITE: Important for activity and substrate specificity; Ala is observed in family members with high D-mannonate dehydratase activity that have no activity with D-gluconate |
Chain | Residue | Details |
A | ALA314 | |
B | ALA314 | |
C | ALA314 | |
D | ALA314 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 9 |
Details | M-CSA 960 |
Chain | Residue | Details |
A | ARG147 | modifies pKa |
A | TYR159 | proton acceptor, proton donor |
A | ASP210 | metal ligand |
A | HIS212 | proton acceptor, proton donor |
A | GLU236 | metal ligand |
A | GLU262 | metal ligand |
A | ARG283 | electrostatic stabiliser |
A | GLU339 | electrostatic stabiliser |
A | TRP402 | modifies pKa |
site_id | MCSA2 |
Number of Residues | 9 |
Details | M-CSA 960 |
Chain | Residue | Details |
B | ARG147 | modifies pKa |
B | TYR159 | proton acceptor, proton donor |
B | ASP210 | metal ligand |
B | HIS212 | proton acceptor, proton donor |
B | GLU236 | metal ligand |
B | GLU262 | metal ligand |
B | ARG283 | electrostatic stabiliser |
B | GLU339 | electrostatic stabiliser |
B | TRP402 | modifies pKa |
site_id | MCSA3 |
Number of Residues | 9 |
Details | M-CSA 960 |
Chain | Residue | Details |
C | ARG147 | modifies pKa |
C | TYR159 | proton acceptor, proton donor |
C | ASP210 | metal ligand |
C | HIS212 | proton acceptor, proton donor |
C | GLU236 | metal ligand |
C | GLU262 | metal ligand |
C | ARG283 | electrostatic stabiliser |
C | GLU339 | electrostatic stabiliser |
C | TRP402 | modifies pKa |
site_id | MCSA4 |
Number of Residues | 9 |
Details | M-CSA 960 |
Chain | Residue | Details |
D | ARG147 | modifies pKa |
D | TYR159 | proton acceptor, proton donor |
D | ASP210 | metal ligand |
D | HIS212 | proton acceptor, proton donor |
D | GLU236 | metal ligand |
D | GLU262 | metal ligand |
D | ARG283 | electrostatic stabiliser |
D | GLU339 | electrostatic stabiliser |
D | TRP402 | modifies pKa |