2CJD
Lysine aminotransferase from M. tuberculosis in external aldimine form
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009450 | biological_process | gamma-aminobutyric acid catabolic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0017000 | biological_process | antibiotic biosynthetic process |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0045484 | molecular_function | L-lysine 6-transaminase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE LYS A 601 |
| Chain | Residue |
| A | VAL63 |
| A | PHE167 |
| A | ARG170 |
| A | GLU243 |
| A | LYS300 |
| A | ASN328 |
| A | THR330 |
| A | PLP1602 |
| A | HOH2271 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PLP A1602 |
| Chain | Residue |
| A | GLY128 |
| A | ALA129 |
| A | PHE167 |
| A | HIS168 |
| A | GLU238 |
| A | ASP271 |
| A | GLN274 |
| A | LYS300 |
| A | SER329 |
| A | THR330 |
| A | LYS601 |
| A | HOH2146 |
| A | HOH2271 |
| A | HOH2272 |
| A | HOH2273 |
| A | HOH2274 |
| A | HOH2275 |
Functional Information from PROSITE/UniProt
| site_id | PS00600 |
| Number of Residues | 38 |
| Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LIfDEVqt.GCgLtGtawayqqldvap....DIVafGKktqVC |
| Chain | Residue | Details |
| A | LEU268-CYS305 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16950391","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26003725","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2CIN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CJD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CJH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2JJE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2JJG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2JJH","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16950391","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2CJD","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16950391","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26003725","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2CJH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2JJH","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"16950391","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26003725","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2CIN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CJH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2JJE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2JJG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2JJH","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1d7r |
| Chain | Residue | Details |
| A | LYS300 | |
| A | PHE167 | |
| A | ASP271 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1d7r |
| Chain | Residue | Details |
| A | ASP97 |
