7S8W
Amycolatopsis sp. T-1-60 N-succinylamino acid racemase/o-succinylbenzoate synthase R266Q mutant in complex with N-succinylphenylglycine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0009234 | biological_process | menaquinone biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0043748 | molecular_function | O-succinylbenzoate synthase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0009234 | biological_process | menaquinone biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0043748 | molecular_function | O-succinylbenzoate synthase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0009234 | biological_process | menaquinone biosynthetic process |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0043748 | molecular_function | O-succinylbenzoate synthase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0009234 | biological_process | menaquinone biosynthetic process |
| D | 0016829 | molecular_function | lyase activity |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0043748 | molecular_function | O-succinylbenzoate synthase activity |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:14705949, ECO:0000305|PubMed:15134446 |
| Chain | Residue | Details |
| A | LYS163 | |
| B | LYS163 | |
| C | LYS163 | |
| D | LYS163 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:14705949, ECO:0000305|PubMed:15134446 |
| Chain | Residue | Details |
| A | LYS263 | |
| B | LYS263 | |
| C | LYS263 | |
| D | LYS263 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15134446, ECO:0007744|PDB:1SJB |
| Chain | Residue | Details |
| A | SER135 | |
| C | LYS161 | |
| C | ASN191 | |
| C | ILE293 | |
| D | SER135 | |
| D | LYS161 | |
| D | ASN191 | |
| D | ILE293 | |
| A | LYS161 | |
| A | ASN191 | |
| A | ILE293 | |
| B | SER135 | |
| B | LYS161 | |
| B | ASN191 | |
| B | ILE293 | |
| C | SER135 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15134446, ECO:0000269|PubMed:23130969, ECO:0000269|Ref.9, ECO:0007744|PDB:1SJA, ECO:0007744|PDB:1SJB, ECO:0007744|PDB:1SJC, ECO:0007744|PDB:4A6G, ECO:0007744|PDB:5FJO, ECO:0007744|PDB:5FJP, ECO:0007744|PDB:5FJR, ECO:0007744|PDB:5FJT, ECO:0007744|PDB:5FJU |
| Chain | Residue | Details |
| A | ASP189 | |
| D | ASP189 | |
| D | GLU214 | |
| D | ASP239 | |
| A | GLU214 | |
| A | ASP239 | |
| B | ASP189 | |
| B | GLU214 | |
| B | ASP239 | |
| C | ASP189 | |
| C | GLU214 | |
| C | ASP239 |
