5BUQ
Unliganded Form of O-succinylbenzoate Coenzyme A Synthetase (MenE) from Bacillus Subtilis, Solved at 1.98 Angstroms
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005524 | molecular_function | ATP binding |
| A | 0008756 | molecular_function | o-succinylbenzoate-CoA ligase activity |
| A | 0009234 | biological_process | menaquinone biosynthetic process |
| A | 0016405 | molecular_function | CoA-ligase activity |
| A | 0016878 | molecular_function | acid-thiol ligase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0008756 | molecular_function | o-succinylbenzoate-CoA ligase activity |
| B | 0009234 | biological_process | menaquinone biosynthetic process |
| B | 0016405 | molecular_function | CoA-ligase activity |
| B | 0016878 | molecular_function | acid-thiol ligase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | binding site for residue ACT B 501 |
| Chain | Residue |
| A | GLU184 |
| B | LEU178 |
| B | ASN179 |
| B | LEU180 |
| B | GLY181 |
| B | HOH732 |
| B | HOH745 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue CA B 502 |
| Chain | Residue |
| B | VAL409 |
| B | HOH662 |
| B | LEU404 |
| B | HIS406 |
Functional Information from PROSITE/UniProt
| site_id | PS00455 |
| Number of Residues | 12 |
| Details | AMP_BINDING Putative AMP-binding domain signature. LMYTSGTTGkPK |
| Chain | Residue | Details |
| A | LEU149-LYS160 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Motif: {"description":"LLG motif","evidences":[{"source":"PubMed","id":"26276389","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27933791","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28559280","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 13 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00731","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26276389","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5BUR","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26276389","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27933791","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5BUS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5GTD","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"28559280","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5X8F","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5X8G","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27933791","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5GTD","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"5X8F","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Site: {"description":"Hinge for 140 degree angle conformational rotation during catalysis","evidences":[{"source":"PubMed","id":"28559280","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 5 |
| Details | Region: {"description":"Required for acetyltransferase recognition","evidences":[{"source":"PubMed","id":"39422507","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine; by AcuA","evidences":[{"source":"PubMed","id":"39422507","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
