4X2P
P. putida mandelate racemase in complex with 3-hydroxypyruvate
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 | 13 |
| Details | binding site for residue 3PY A 401 |
| Chain | Residue |
| A | SER139 |
| A | MG402 |
| A | HOH548 |
| A | HOH626 |
| A | HOH750 |
| A | LYS164 |
| A | LYS166 |
| A | ASP195 |
| A | GLU221 |
| A | GLU247 |
| A | HIS297 |
| A | GLU317 |
| A | LEU319 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 402 |
| Chain | Residue |
| A | ASP195 |
| A | GLU221 |
| A | GLU247 |
| A | 3PY401 |
| A | HOH726 |
| A | HOH750 |
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 | 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 |
