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 |