2MNR
MECHANISM OF THE REACTION CATALYZED BY MANDELATE RACEMASE. 2. CRYSTAL STRUCTURE OF MANDELATE RACEMASE AT 2.5 ANGSTROMS RESOLUTION: IDENTIFICATION OF THE ACTIVE SITE AND POSSIBLE CATALYTIC RESIDUES
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN A 360 |
| Chain | Residue |
| A | GLU247 |
| A | SO4361 |
| A | HOH414 |
| A | HOH459 |
| A | ASP195 |
| A | GLU221 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE SO4 A 361 |
| Chain | Residue |
| A | SER139 |
| A | LYS164 |
| A | LYS166 |
| A | ASP195 |
| A | GLU221 |
| A | GLU247 |
| A | HIS297 |
| A | GLU317 |
| A | MN360 |
| A | HOH434 |
| A | HOH459 |
| A | HOH617 |
| site_id | ACT |
| Number of Residues | 2 |
| Details | ACID/BASE CATALYSTS RESPONSIBLE FOR PROTON ABSTRACTION AND REDELIVERY IN THE RACEMIZATION REACTION |
| Chain | Residue |
| A | LYS166 |
| A | HIS297 |
| site_id | CAR |
| Number of Residues | 2 |
| Details | 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 | 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 | Active site: {"description":"Proton acceptor; specific for S-mandelate"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor; specific for R-mandelate"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| 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 | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1mdr |
| Chain | Residue | Details |
| A | GLU317 | |
| A | LYS166 | |
| A | HIS297 | |
| A | ASP270 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1mdr |
| Chain | Residue | Details |
| A | LYS164 | |
| A | LYS166 | |
| A | SER324 |
| 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 |
