1MDL
MANDELATE RACEMASE MUTANT K166R CO-CRYSTALLIZED WITH (R)-MANDELATE
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 360 |
| Chain | Residue |
| A | GLU247 |
| A | SMN399 |
| A | HOH465 |
| A | ASP195 |
| A | GLU221 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE RMN A 398 |
| Chain | Residue |
| A | THR24 |
| A | VAL29 |
| A | PHE52 |
| A | LEU93 |
| A | ARG166 |
| A | SMN399 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE SMN A 399 |
| Chain | Residue |
| A | PHE52 |
| A | LYS164 |
| A | ARG166 |
| A | ASP195 |
| A | ASN197 |
| A | GLU221 |
| A | GLU247 |
| A | HIS297 |
| A | GLU317 |
| A | MG360 |
| A | RMN398 |
| A | HOH465 |
| A | HOH480 |
| site_id | ACT |
| Number of Residues | 2 |
| Details | SITE ACT CONSTITUTES THE ACID/BASE CATALYSTS RESPONSIBLE FOR PROTON ABSTRACTION AND REDELIVERY IN THE RACEMIZATION REACTION. |
| Chain | Residue |
| A | ARG166 |
| A | HIS297 |
| site_id | CAR |
| Number of Residues | 2 |
| Details | SITE CAR CONSTITUTES THE BINDING SITE FOR THE CARBOXYL GROUP OF SUBSTRATE. THESE RESIDUES FUNCTION, ALONG WITH THE METAL ION, AS ELECTROPHILIC CATALYSTS. |
| Chain | Residue |
| A | LYS164 |
| A | GLU317 |
| site_id | MTL |
| Number of Residues | 3 |
| Details | SITE MTL CONSTITUTES THE DIRECT METAL ION LIGANDS. |
| Chain | Residue |
| A | ASP195 |
| A | GLU221 |
| A | GLU247 |
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 | 1 |
| Details | ACT_SITE: Proton acceptor; specific for S-mandelate |
| Chain | Residue | Details |
| A | ARG166 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor; specific for R-mandelate |
| Chain | Residue | Details |
| A | HIS297 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:7893689, ECO:0000269|PubMed:7893690, ECO:0000305|PubMed:1892834 |
| Chain | Residue | Details |
| A | ASP195 | |
| A | GLU221 | |
| A | GLU247 | |
| A | GLU317 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1mdr |
| Chain | Residue | Details |
| A | GLU317 | |
| A | ARG166 | |
| A | HIS297 | |
| A | ASP270 |
| site_id | MCSA1 |
| Number of Residues | 9 |
| Details | M-CSA 187 |
| Chain | Residue | Details |
| A | LYS164 | electrostatic stabiliser, hydrogen bond donor |
| A | ARG166 | 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 |
