3TFT
Crystal structure of 7,8-diaminopelargonic acid synthase (BioA) from Mycobacterium tuberculosis, pre-reaction complex with a 3,6-dihydropyrid-2-one heterocycle inhibitor
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004015 | molecular_function | adenosylmethionine-8-amino-7-oxononanoate transaminase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009102 | biological_process | biotin biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0004015 | molecular_function | adenosylmethionine-8-amino-7-oxononanoate transaminase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0009102 | biological_process | biotin biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP A 501 |
| Chain | Residue |
| A | GLY124 |
| A | HOH466 |
| A | HOH574 |
| B | PRO317 |
| B | THR318 |
| B | HOH567 |
| A | SER125 |
| A | TYR157 |
| A | HIS158 |
| A | GLU220 |
| A | ASP254 |
| A | ILE256 |
| A | ALA257 |
| A | LYS283 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PLP B 501 |
| Chain | Residue |
| A | PRO317 |
| A | THR318 |
| A | HOH462 |
| B | GLY124 |
| B | SER125 |
| B | TYR157 |
| B | HIS158 |
| B | GLY159 |
| B | GLU220 |
| B | ASP254 |
| B | ILE256 |
| B | ALA257 |
| B | LYS283 |
| B | HOH469 |
| B | HOH515 |
| B | HOH682 |
| B | HOH769 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE DMS A 438 |
| Chain | Residue |
| A | TYR25 |
| A | TRP64 |
| A | ARG400 |
| A | HOH672 |
| A | HOH849 |
| B | GLY93 |
Functional Information from PROSITE/UniProt
| site_id | PS00600 |
| Number of Residues | 38 |
| Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LIfDEIat.GFgRtGalfaadhagvsp....DIMcvGKaltGG |
| Chain | Residue | Details |
| A | LEU251-GLY288 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20565114","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00834","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20565114","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Site: {"description":"Participates in the substrate recognition with KAPA and in a stacking interaction with the adenine ring of SAM","evidences":[{"source":"PubMed","id":"20565114","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"20565114","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3BV0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3LV2","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
