2A7P
Crystal Structure of the G81A mutant of the Active Chimera of (S)-Mandelate Dehydrogenase in complex with its substrate 3-indolelactate
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE FMN A 390 |
| Chain | Residue |
| A | TYR26 |
| A | LYS231 |
| A | SER253 |
| A | HIS255 |
| A | GLY256 |
| A | ARG258 |
| A | ASP284 |
| A | SER285 |
| A | GLY286 |
| A | ARG288 |
| A | GLY307 |
| A | LEU27 |
| A | ARG308 |
| A | 3IL410 |
| A | HOH895 |
| A | HOH896 |
| A | HOH902 |
| A | HOH937 |
| A | PRO79 |
| A | THR80 |
| A | ALA81 |
| A | SER108 |
| A | GLN129 |
| A | TYR131 |
| A | THR156 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MES A 890 |
| Chain | Residue |
| A | TRP87 |
| A | LYS89 |
| A | ASP240 |
| A | ILE243 |
| A | LYS276 |
| A | THR277 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE 3IL A 410 |
| Chain | Residue |
| A | ALA110 |
| A | TYR131 |
| A | ARG165 |
| A | HIS255 |
| A | FMN390 |
| A | HOH966 |
| A | HOH980 |
| A | HOH981 |
| A | HOH995 |
Functional Information from PROSITE/UniProt
| site_id | PS00557 |
| Number of Residues | 7 |
| Details | FMN_HYDROXY_ACID_DH_1 FMN-dependent alpha-hydroxy acid dehydrogenases active site. SNHGGRQ |
| Chain | Residue | Details |
| A | SER253-GLN259 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00683","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19465768","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2A85","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 11 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"14604988","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30071260","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1P4C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6BFG","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"2681790","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9144771","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AL7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GOX","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Site: {"description":"Involved in determining the substrate specificity of glycolate oxidase","evidences":[{"source":"PubMed","id":"7705356","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1fcb |
| Chain | Residue | Details |
| A | TYR131 | |
| A | ASP158 | |
| A | HIS255 | |
| A | ARG258 | |
| A | TYR26 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1fcb |
| Chain | Residue | Details |
| A | TYR131 | |
| A | HIS255 | |
| A | ARG258 | |
| A | ASP158 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 852 |
| Chain | Residue | Details |
| A | SER108 | electrostatic stabiliser |
| A | TYR131 | electrostatic stabiliser, modifies pKa |
| A | THR156 | electrostatic stabiliser |
| A | LYS231 | electrostatic stabiliser, enhance reactivity |
| A | HIS255 | proton shuttle (general acid/base) |
