3UXK
P. putida mandelate racemase co-crystallized with the intermediate analogue benzohydroxamate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0009063 | biological_process | amino acid 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 | 0009063 | biological_process | amino acid 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 | 0009063 | biological_process | amino acid 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 | 0009063 | biological_process | amino acid 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 360 |
| Chain | Residue |
| A | ASP195 |
| A | GLU221 |
| A | GLU247 |
| A | BHO361 |
| A | HOH722 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE BHO A 361 |
| Chain | Residue |
| A | GLU221 |
| A | GLU247 |
| A | HIS297 |
| A | GLU317 |
| A | MG360 |
| A | HOH722 |
| A | LYS164 |
| A | LYS166 |
| A | ASP195 |
| A | ASN197 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 360 |
| Chain | Residue |
| B | ASP195 |
| B | GLU221 |
| B | GLU247 |
| B | BHO361 |
| B | HOH723 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE BHO B 361 |
| Chain | Residue |
| B | LYS164 |
| B | LYS166 |
| B | ASP195 |
| B | ASN197 |
| B | GLU221 |
| B | GLU247 |
| B | HIS297 |
| B | GLU317 |
| B | MG360 |
| B | HOH723 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 360 |
| Chain | Residue |
| C | ASP195 |
| C | GLU221 |
| C | GLU247 |
| C | BHO361 |
| C | HOH721 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE BHO C 361 |
| Chain | Residue |
| C | LYS164 |
| C | LYS166 |
| C | ASP195 |
| C | ASN197 |
| C | GLU221 |
| C | GLU247 |
| C | HIS297 |
| C | GLU317 |
| C | MG360 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 360 |
| Chain | Residue |
| D | ASP195 |
| D | GLU221 |
| D | GLU247 |
| D | BHO361 |
| D | HOH724 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE BHO D 361 |
| Chain | Residue |
| D | LYS164 |
| D | LYS166 |
| D | ASP195 |
| D | ASN197 |
| D | GLU221 |
| D | GLU247 |
| D | HIS297 |
| D | GLU317 |
| D | MG360 |
| D | HOH724 |
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 | 4 |
| Details | ACT_SITE: Proton acceptor; specific for S-mandelate |
| Chain | Residue | Details |
| A | LYS166 | |
| B | LYS166 | |
| C | LYS166 | |
| D | LYS166 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor; specific for R-mandelate |
| Chain | Residue | Details |
| A | HIS297 | |
| B | HIS297 | |
| C | HIS297 | |
| D | HIS297 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| 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 | |
| A | GLU221 | |
| A | GLU247 | |
| 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 |
