1MDR
THE ROLE OF LYSINE 166 IN THE MECHANISM OF MANDELATE RACEMASE FROM PSEUDOMONAS PUTIDA: MECHANISTIC AND CRYSTALLOGRAPHIC EVIDENCE FOR STEREOSPECIFIC ALKYLATION BY (R)-ALPHA-PHENYLGLYCIDATE
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 | 5 |
Details | BINDING SITE FOR RESIDUE MG A 360 |
Chain | Residue |
A | GLU247 |
A | APG399 |
A | HOH414 |
A | ASP195 |
A | GLU221 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE APG A 399 |
Chain | Residue |
A | LYS164 |
A | LYS166 |
A | ASP195 |
A | ASN197 |
A | GLU221 |
A | GLU247 |
A | HIS297 |
A | GLU317 |
A | MG360 |
A | HOH414 |
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 | 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 | ACT_SITE: Proton acceptor; specific for S-mandelate |
Chain | Residue | Details |
A | LYS166 |
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 | a catalytic site defined by CSA, PubMed 1892834, 7893689, 7893690 |
Chain | Residue | Details |
A | GLU317 | |
A | LYS166 | |
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 | 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 |