4WYD
Adenosylmethionine-8-amino-7-oxononanoate aminotransferase from Mycobacterium tuberculosis complexed with a fragment from DSF screening
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 | 17 |
| Details | binding site for residue PLP A 501 |
| Chain | Residue |
| A | TRP65 |
| A | 3VR502 |
| A | HOH622 |
| A | HOH737 |
| A | HOH741 |
| A | HOH784 |
| B | GLY316 |
| B | PRO317 |
| B | THR318 |
| A | SER125 |
| A | TYR157 |
| A | HIS158 |
| A | GLU220 |
| A | ASP254 |
| A | ILE256 |
| A | ALA257 |
| A | LYS283 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | binding site for residue 3VR A 502 |
| Chain | Residue |
| A | TYR25 |
| A | TRP64 |
| A | TRP65 |
| A | TYR157 |
| A | MET174 |
| A | ALA226 |
| A | PLP501 |
| A | EPE503 |
| A | HOH644 |
| B | GLY316 |
| B | THR318 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | binding site for residue EPE A 503 |
| Chain | Residue |
| A | TYR25 |
| A | SER27 |
| A | GLU31 |
| A | TRP64 |
| A | ARG400 |
| A | 3VR502 |
| A | HOH676 |
| A | HOH707 |
| A | HOH714 |
| B | GLY93 |
| B | GLY94 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 504 |
| Chain | Residue |
| A | ARG193 |
| A | ARG230 |
| A | PHE231 |
| A | ARG369 |
| A | HOH612 |
| A | HOH860 |
| A | HOH917 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 505 |
| Chain | Residue |
| A | PRO234 |
| A | CYS371 |
| A | HOH611 |
| A | HOH890 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | binding site for residue EDO A 506 |
| Chain | Residue |
| A | ARG142 |
| A | LEU144 |
| A | HOH615 |
| A | HOH641 |
| A | HOH812 |
| B | ARG154 |
| B | GLN185 |
| B | VAL186 |
| B | PHE187 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 507 |
| Chain | Residue |
| A | GLY355 |
| A | THR358 |
| A | THR423 |
| A | SER424 |
| A | HOH620 |
| B | ARG85 |
| B | HOH829 |
| B | HOH935 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 508 |
| Chain | Residue |
| A | ARG241 |
| A | ARG245 |
| A | HOH638 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 509 |
| Chain | Residue |
| A | ILE110 |
| A | THR111 |
| A | PRO112 |
| A | ALA113 |
| A | ASP270 |
| A | EDO510 |
| B | ARG235 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 510 |
| Chain | Residue |
| A | ASP270 |
| A | EDO509 |
| B | ARG235 |
| B | HIS238 |
| site_id | AD2 |
| Number of Residues | 11 |
| Details | binding site for residue 3VR B 502 |
| Chain | Residue |
| A | GLY316 |
| A | THR318 |
| B | TYR25 |
| B | TRP64 |
| B | TRP65 |
| B | TYR157 |
| B | ALA226 |
| B | PHE402 |
| B | PLP501 |
| B | EPE503 |
| B | HOH634 |
| site_id | AD3 |
| Number of Residues | 11 |
| Details | binding site for residue EPE B 503 |
| Chain | Residue |
| B | 3VR502 |
| B | HOH660 |
| B | HOH683 |
| B | HOH729 |
| A | GLY93 |
| A | GLY94 |
| B | TYR25 |
| B | SER27 |
| B | GLU31 |
| B | TRP64 |
| B | ARG400 |
| site_id | AD4 |
| Number of Residues | 8 |
| Details | binding site for residue EDO B 504 |
| Chain | Residue |
| A | ARG403 |
| A | ASN404 |
| B | GLN53 |
| B | ILE55 |
| B | HOH687 |
| B | HOH734 |
| B | HOH809 |
| B | HOH851 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 505 |
| Chain | Residue |
| B | ARG193 |
| B | ARG230 |
| B | PHE231 |
| B | ARG369 |
| B | HOH614 |
| B | HOH684 |
| site_id | AD6 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 506 |
| Chain | Residue |
| B | TRP45 |
| B | GLU56 |
| site_id | AD7 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 507 |
| Chain | Residue |
| B | ARG193 |
| B | ASP194 |
| site_id | AD8 |
| Number of Residues | 25 |
| Details | binding site for Di-peptide PLP B 501 and LYS B 283 |
| Chain | Residue |
| A | GLY316 |
| A | PRO317 |
| A | THR318 |
| A | PHE319 |
| B | TRP64 |
| B | TRP65 |
| B | GLY124 |
| B | SER125 |
| B | TYR157 |
| B | HIS158 |
| B | GLU220 |
| B | ASP254 |
| B | ILE256 |
| B | ALA257 |
| B | GLY282 |
| B | ALA284 |
| B | LEU285 |
| B | THR286 |
| B | 3VR502 |
| B | HOH616 |
| B | HOH669 |
| B | HOH704 |
| B | HOH708 |
| B | HOH761 |
| B | HOH817 |
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 |
