4FP1
P. putida mandelate racemase co-crystallized with 3,3,3-trifluoro-2-hydroxy-2-(trifluoromethyl) propionic 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG A 401 |
| Chain | Residue |
| A | ASP195 |
| A | GLU221 |
| A | GLU247 |
| A | BFM402 |
| A | HOH730 |
| A | HOH732 |
| A | HOH733 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE BFM A 402 |
| Chain | Residue |
| A | VAL29 |
| A | PHE52 |
| A | LYS166 |
| A | ASN197 |
| A | GLU247 |
| A | HIS297 |
| A | LEU298 |
| A | LEU319 |
| A | MG401 |
| A | HOH732 |
| A | HOH733 |
| A | HOH750 |
| B | LEU93 |
| A | VAL22 |
| A | THR24 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG B 401 |
| Chain | Residue |
| B | ASP195 |
| B | GLU221 |
| B | GLU247 |
| B | BFM402 |
| B | HOH681 |
| B | HOH682 |
| B | HOH687 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE BFM B 402 |
| Chain | Residue |
| A | LEU93 |
| B | VAL22 |
| B | THR24 |
| B | VAL29 |
| B | PHE52 |
| B | LYS166 |
| B | ASN197 |
| B | GLU247 |
| B | HIS297 |
| B | LEU298 |
| B | LEU319 |
| B | MG401 |
| B | HOH682 |
| B | HOH687 |
| B | HOH689 |
| B | HOH690 |
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 | 2 |
| Details | Active site: {"description":"Proton acceptor; specific for S-mandelate"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor; specific for R-mandelate"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"7893689","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7893690","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1892834","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
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 |
