4WYA
Crystal structure of 7,8-diaminopelargonic acid synthase (BioA) from Mycobacterium tuberculosis, complexed with a fragment hit
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 |
| C | 0004015 | molecular_function | adenosylmethionine-8-amino-7-oxononanoate transaminase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0009102 | biological_process | biotin biosynthetic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0004015 | molecular_function | adenosylmethionine-8-amino-7-oxononanoate transaminase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0008483 | molecular_function | transaminase activity |
| D | 0009102 | biological_process | biotin biosynthetic process |
| D | 0016740 | molecular_function | transferase activity |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | binding site for residue PLP A 501 |
| Chain | Residue |
| A | SER123 |
| A | HOH608 |
| B | PRO317 |
| B | THR318 |
| A | GLY124 |
| A | SER125 |
| A | TYR157 |
| A | HIS158 |
| A | GLU220 |
| A | ASP254 |
| A | ILE256 |
| A | ALA257 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue 3VQ B 501 |
| Chain | Residue |
| A | PRO24 |
| A | TRP64 |
| A | PHE402 |
| B | MET91 |
| B | PHE92 |
| B | GLY93 |
| B | GLY316 |
| B | PRO317 |
| B | THR318 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | binding site for residue PLP B 502 |
| Chain | Residue |
| A | PRO317 |
| A | THR318 |
| B | SER123 |
| B | GLY124 |
| B | SER125 |
| B | TYR157 |
| B | HIS158 |
| B | GLY159 |
| B | GLU220 |
| B | ASP254 |
| B | ILE256 |
| B | ALA257 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | binding site for residue PLP C 501 |
| Chain | Residue |
| C | SER123 |
| C | GLY124 |
| C | SER125 |
| C | TYR157 |
| C | HIS158 |
| C | GLU220 |
| C | ASP254 |
| C | ILE256 |
| C | ALA257 |
| D | THR318 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue 3VQ D 501 |
| Chain | Residue |
| C | TYR25 |
| C | TRP64 |
| D | MET91 |
| D | PHE92 |
| D | GLY93 |
| D | GLY316 |
| D | PRO317 |
| D | THR318 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | binding site for residue PLP D 502 |
| Chain | Residue |
| C | PRO317 |
| C | THR318 |
| D | GLY124 |
| D | SER125 |
| D | TYR157 |
| D | HIS158 |
| D | GLU220 |
| D | ASP254 |
| D | ILE256 |
| D | ALA257 |
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 | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20565114 |
| Chain | Residue | Details |
| A | TRP64 | |
| D | TRP64 | |
| D | TYR157 | |
| D | GLY316 | |
| A | TYR157 | |
| A | GLY316 | |
| B | TRP64 | |
| B | TYR157 | |
| B | GLY316 | |
| C | TRP64 | |
| C | TYR157 | |
| C | GLY316 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00834 |
| Chain | Residue | Details |
| A | GLY124 | |
| C | ASP254 | |
| C | LYS283 | |
| C | PRO317 | |
| D | GLY124 | |
| D | ASP254 | |
| D | LYS283 | |
| D | PRO317 | |
| A | ASP254 | |
| A | LYS283 | |
| A | PRO317 | |
| B | GLY124 | |
| B | ASP254 | |
| B | LYS283 | |
| B | PRO317 | |
| C | GLY124 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:20565114 |
| Chain | Residue | Details |
| A | ARG400 | |
| B | ARG400 | |
| C | ARG400 | |
| D | ARG400 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | SITE: Participates in the substrate recognition with KAPA and in a stacking interaction with the adenine ring of SAM => ECO:0000305|PubMed:20565114 |
| Chain | Residue | Details |
| A | TYR25 | |
| B | TYR25 | |
| C | TYR25 | |
| D | TYR25 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:20565114, ECO:0007744|PDB:3BV0, ECO:0007744|PDB:3LV2 |
| Chain | Residue | Details |
| A | LYS283 | |
| B | LYS283 | |
| C | LYS283 | |
| D | LYS283 |
