4XJP
Crystal structure of 7,8-diaminopelargonic acid synthase (BioA) from Mycobacterium tuberculosis, complexed with an inhibitor optimized from HTS lead
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 | 18 |
| Details | binding site for residue PLP A 501 |
| Chain | Residue |
| A | GLY124 |
| A | LYS283 |
| A | HOH733 |
| A | HOH755 |
| A | HOH764 |
| A | HOH774 |
| A | HOH872 |
| B | PRO317 |
| B | THR318 |
| B | HOH688 |
| A | SER125 |
| A | TYR157 |
| A | HIS158 |
| A | GLY159 |
| A | GLU220 |
| A | ASP254 |
| A | ILE256 |
| A | ALA257 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | binding site for residue 41N A 502 |
| Chain | Residue |
| A | TYR25 |
| A | TRP64 |
| A | GLY156 |
| A | TYR157 |
| A | CYS168 |
| A | GLY172 |
| A | GLY173 |
| A | ALA226 |
| A | GLY227 |
| A | ARG400 |
| A | PHE402 |
| A | HOH779 |
| A | HOH798 |
| B | MET91 |
| B | PHE92 |
| B | GLY93 |
| B | GLY316 |
| B | PRO317 |
| B | THR318 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 503 |
| Chain | Residue |
| A | LEU385 |
| A | PHE402 |
| A | ARG403 |
| A | HOH815 |
| A | HOH893 |
| A | HOH1022 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue PEG A 504 |
| Chain | Residue |
| A | ARG193 |
| A | VAL222 |
| A | HIS232 |
| A | ASP233 |
| A | PRO234 |
| A | HOH1066 |
| A | HOH1067 |
| site_id | AC5 |
| Number of Residues | 19 |
| Details | binding site for residue 41N B 502 |
| Chain | Residue |
| A | MET91 |
| A | PHE92 |
| A | GLY93 |
| A | GLY316 |
| A | PRO317 |
| A | THR318 |
| B | TYR25 |
| B | TRP64 |
| B | GLY156 |
| B | TYR157 |
| B | CYS168 |
| B | GLY172 |
| B | GLY173 |
| B | ALA226 |
| B | GLY227 |
| B | ARG400 |
| B | PHE402 |
| B | HOH773 |
| B | HOH920 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 503 |
| Chain | Residue |
| B | GLU56 |
| B | HOH610 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | binding site for residue EDO B 504 |
| Chain | Residue |
| A | ASP122 |
| A | PHE319 |
| A | HOH737 |
| B | ASP122 |
| B | SER123 |
| B | GLY282 |
| B | SER291 |
| B | LEU292 |
| B | HOH798 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 505 |
| Chain | Residue |
| B | GLY355 |
| B | THR358 |
| B | THR420 |
| B | THR423 |
| B | SER424 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue PEG B 506 |
| Chain | Residue |
| B | ARG193 |
| B | HIS232 |
| B | ASP233 |
| B | PRO234 |
| B | HIS271 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 507 |
| Chain | Residue |
| A | HIS271 |
| A | ALA272 |
| B | ARG246 |
| B | TYR247 |
| site_id | AD2 |
| Number of Residues | 23 |
| Details | binding site for Di-peptide PLP B 501 and LYS B 283 |
| Chain | Residue |
| B | THR66 |
| B | GLY124 |
| B | SER125 |
| B | TYR157 |
| B | HIS158 |
| B | GLY159 |
| B | GLU220 |
| B | ASP254 |
| B | ILE256 |
| B | ALA257 |
| B | GLY282 |
| B | ALA284 |
| B | LEU285 |
| B | HOH710 |
| B | HOH720 |
| B | HOH725 |
| B | HOH749 |
| B | HOH798 |
| A | PRO317 |
| A | THR318 |
| A | HOH737 |
| B | TRP64 |
| B | TRP65 |
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 |
