7MQX
P. putida mandelate racemase forms an oxobenzoxaborole adduct with 2-formylphenylboronic acid
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0009063 | biological_process | amino acid catabolic process |
A | 0016052 | biological_process | carbohydrate catabolic process |
A | 0016836 | molecular_function | hydro-lyase activity |
A | 0016853 | molecular_function | isomerase activity |
A | 0018838 | molecular_function | mandelate racemase activity |
A | 0018924 | biological_process | mandelate metabolic process |
A | 0019596 | biological_process | mandelate catabolic process |
A | 0046872 | molecular_function | metal ion binding |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0009063 | biological_process | amino acid catabolic process |
B | 0016052 | biological_process | carbohydrate catabolic process |
B | 0016836 | molecular_function | hydro-lyase activity |
B | 0016853 | molecular_function | isomerase activity |
B | 0018838 | molecular_function | mandelate racemase activity |
B | 0018924 | biological_process | mandelate metabolic process |
B | 0019596 | biological_process | mandelate catabolic process |
B | 0046872 | molecular_function | metal ion binding |
C | 0000287 | molecular_function | magnesium ion binding |
C | 0009063 | biological_process | amino acid catabolic process |
C | 0016052 | biological_process | carbohydrate catabolic process |
C | 0016836 | molecular_function | hydro-lyase activity |
C | 0016853 | molecular_function | isomerase activity |
C | 0018838 | molecular_function | mandelate racemase activity |
C | 0018924 | biological_process | mandelate metabolic process |
C | 0019596 | biological_process | mandelate catabolic process |
C | 0046872 | molecular_function | metal ion binding |
D | 0000287 | molecular_function | magnesium ion binding |
D | 0009063 | biological_process | amino acid catabolic process |
D | 0016052 | biological_process | carbohydrate catabolic process |
D | 0016836 | molecular_function | hydro-lyase activity |
D | 0016853 | molecular_function | isomerase activity |
D | 0018838 | molecular_function | mandelate racemase activity |
D | 0018924 | biological_process | mandelate metabolic process |
D | 0019596 | biological_process | mandelate catabolic process |
D | 0046872 | molecular_function | metal ion binding |
E | 0000287 | molecular_function | magnesium ion binding |
E | 0009063 | biological_process | amino acid catabolic process |
E | 0016052 | biological_process | carbohydrate catabolic process |
E | 0016836 | molecular_function | hydro-lyase activity |
E | 0016853 | molecular_function | isomerase activity |
E | 0018838 | molecular_function | mandelate racemase activity |
E | 0018924 | biological_process | mandelate metabolic process |
E | 0019596 | biological_process | mandelate catabolic process |
E | 0046872 | molecular_function | metal ion binding |
F | 0000287 | molecular_function | magnesium ion binding |
F | 0009063 | biological_process | amino acid catabolic process |
F | 0016052 | biological_process | carbohydrate catabolic process |
F | 0016836 | molecular_function | hydro-lyase activity |
F | 0016853 | molecular_function | isomerase activity |
F | 0018838 | molecular_function | mandelate racemase activity |
F | 0018924 | biological_process | mandelate metabolic process |
F | 0019596 | biological_process | mandelate catabolic process |
F | 0046872 | molecular_function | metal ion binding |
G | 0000287 | molecular_function | magnesium ion binding |
G | 0009063 | biological_process | amino acid catabolic process |
G | 0016052 | biological_process | carbohydrate catabolic process |
G | 0016836 | molecular_function | hydro-lyase activity |
G | 0016853 | molecular_function | isomerase activity |
G | 0018838 | molecular_function | mandelate racemase activity |
G | 0018924 | biological_process | mandelate metabolic process |
G | 0019596 | biological_process | mandelate catabolic process |
G | 0046872 | molecular_function | metal ion binding |
H | 0000287 | molecular_function | magnesium ion binding |
H | 0009063 | biological_process | amino acid catabolic process |
H | 0016052 | biological_process | carbohydrate catabolic process |
H | 0016836 | molecular_function | hydro-lyase activity |
H | 0016853 | molecular_function | isomerase activity |
H | 0018838 | molecular_function | mandelate racemase activity |
H | 0018924 | biological_process | mandelate metabolic process |
H | 0019596 | biological_process | mandelate catabolic process |
H | 0046872 | molecular_function | metal ion binding |
Functional Information from PROSITE/UniProt
site_id | PS00908 |
Number of Residues | 26 |
Details | MR_MLE_1 Mandelate racemase / muconate lactonizing enzyme family signature 1. AaAGIDmAAwDAlGKvhetPLvkLLG |
Chain | Residue | Details |
A | ALA103-GLY128 |
site_id | PS00909 |
Number of Residues | 32 |
Details | MR_MLE_2 Mandelate racemase / muconate lactonizing enzyme family signature 2. ImvDyNqsldvpaAikrsqaLqqegvtwIEEP |
Chain | Residue | Details |
A | ILE192-PRO223 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | ACT_SITE: Proton acceptor; specific for S-mandelate |
Chain | Residue | Details |
A | LYS166 | |
B | LYS166 | |
C | LYS166 | |
D | LYS166 | |
E | LYS166 | |
F | LYS166 | |
G | LYS166 | |
H | LYS166 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | ACT_SITE: Proton acceptor; specific for R-mandelate |
Chain | Residue | Details |
A | HIS297 | |
B | HIS297 | |
C | HIS297 | |
D | HIS297 | |
E | HIS297 | |
F | HIS297 | |
G | HIS297 | |
H | HIS297 |
site_id | SWS_FT_FI3 |
Number of Residues | 32 |
Details | BINDING: BINDING => ECO:0000269|PubMed:7893689, ECO:0000269|PubMed:7893690, ECO:0000305|PubMed:1892834 |
Chain | Residue | Details |
A | ASP195 | |
C | GLU221 | |
C | GLU247 | |
C | GLU317 | |
D | ASP195 | |
D | GLU221 | |
D | GLU247 | |
D | GLU317 | |
E | ASP195 | |
E | GLU221 | |
E | GLU247 | |
A | GLU221 | |
E | GLU317 | |
F | ASP195 | |
F | GLU221 | |
F | GLU247 | |
F | GLU317 | |
G | ASP195 | |
G | GLU221 | |
G | GLU247 | |
G | GLU317 | |
H | ASP195 | |
A | GLU247 | |
H | GLU221 | |
H | GLU247 | |
H | GLU317 | |
A | GLU317 | |
B | ASP195 | |
B | GLU221 | |
B | GLU247 | |
B | GLU317 | |
C | ASP195 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 9 |
Details | M-CSA 187 |
Chain | Residue | Details |
A | LYS164 | electrostatic stabiliser, hydrogen bond donor |
A | LYS166 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | ASP195 | metal ligand |
A | ASN197 | electrostatic stabiliser |
A | GLU221 | metal ligand |
A | GLU247 | metal ligand |
A | ASP270 | electrostatic stabiliser, hydrogen bond acceptor, increase basicity |
A | HIS297 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | GLU317 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
site_id | MCSA2 |
Number of Residues | 9 |
Details | M-CSA 187 |
Chain | Residue | Details |
B | LYS164 | electrostatic stabiliser, hydrogen bond donor |
B | LYS166 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
B | ASP195 | metal ligand |
B | ASN197 | electrostatic stabiliser |
B | GLU221 | metal ligand |
B | GLU247 | metal ligand |
B | ASP270 | electrostatic stabiliser, hydrogen bond acceptor, increase basicity |
B | HIS297 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
B | GLU317 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
site_id | MCSA3 |
Number of Residues | 9 |
Details | M-CSA 187 |
Chain | Residue | Details |
C | LYS164 | electrostatic stabiliser, hydrogen bond donor |
C | LYS166 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
C | ASP195 | metal ligand |
C | ASN197 | electrostatic stabiliser |
C | GLU221 | metal ligand |
C | GLU247 | metal ligand |
C | ASP270 | electrostatic stabiliser, hydrogen bond acceptor, increase basicity |
C | HIS297 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
C | GLU317 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
site_id | MCSA4 |
Number of Residues | 9 |
Details | M-CSA 187 |
Chain | Residue | Details |
D | LYS164 | electrostatic stabiliser, hydrogen bond donor |
D | LYS166 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
D | ASP195 | metal ligand |
D | ASN197 | electrostatic stabiliser |
D | GLU221 | metal ligand |
D | GLU247 | metal ligand |
D | ASP270 | electrostatic stabiliser, hydrogen bond acceptor, increase basicity |
D | HIS297 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
D | GLU317 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
site_id | MCSA5 |
Number of Residues | 9 |
Details | M-CSA 187 |
Chain | Residue | Details |
E | LYS164 | electrostatic stabiliser, hydrogen bond donor |
E | LYS166 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
E | ASP195 | metal ligand |
E | ASN197 | electrostatic stabiliser |
E | GLU221 | metal ligand |
E | GLU247 | metal ligand |
E | ASP270 | electrostatic stabiliser, hydrogen bond acceptor, increase basicity |
E | HIS297 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
E | GLU317 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
site_id | MCSA6 |
Number of Residues | 9 |
Details | M-CSA 187 |
Chain | Residue | Details |
F | LYS164 | electrostatic stabiliser, hydrogen bond donor |
F | LYS166 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
F | ASP195 | metal ligand |
F | ASN197 | electrostatic stabiliser |
F | GLU221 | metal ligand |
F | GLU247 | metal ligand |
F | ASP270 | electrostatic stabiliser, hydrogen bond acceptor, increase basicity |
F | HIS297 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
F | GLU317 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
site_id | MCSA7 |
Number of Residues | 9 |
Details | M-CSA 187 |
Chain | Residue | Details |
G | LYS164 | electrostatic stabiliser, hydrogen bond donor |
G | LYS166 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
G | ASP195 | metal ligand |
G | ASN197 | electrostatic stabiliser |
G | GLU221 | metal ligand |
G | GLU247 | metal ligand |
G | ASP270 | electrostatic stabiliser, hydrogen bond acceptor, increase basicity |
G | HIS297 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
G | GLU317 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
site_id | MCSA8 |
Number of Residues | 9 |
Details | M-CSA 187 |
Chain | Residue | Details |
H | LYS164 | electrostatic stabiliser, hydrogen bond donor |
H | LYS166 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
H | ASP195 | metal ligand |
H | ASN197 | electrostatic stabiliser |
H | GLU221 | metal ligand |
H | GLU247 | metal ligand |
H | ASP270 | electrostatic stabiliser, hydrogen bond acceptor, increase basicity |
H | HIS297 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
H | GLU317 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |