5YHV
Crystal structure of an aminotransferase from Mycobacterium tuberculosis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009042 | molecular_function | valine-pyruvate transaminase activity |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0009274 | cellular_component | peptidoglycan-based cell wall |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0009042 | molecular_function | valine-pyruvate transaminase activity |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0009274 | cellular_component | peptidoglycan-based cell wall |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0009042 | molecular_function | valine-pyruvate transaminase activity |
| C | 0009058 | biological_process | biosynthetic process |
| C | 0009274 | cellular_component | peptidoglycan-based cell wall |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0008483 | molecular_function | transaminase activity |
| D | 0009042 | molecular_function | valine-pyruvate transaminase activity |
| D | 0009058 | biological_process | biosynthetic process |
| D | 0009274 | cellular_component | peptidoglycan-based cell wall |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | binding site for residue GLU A 401 |
| Chain | Residue |
| A | ASP80 |
| A | TYR81 |
| A | HIS85 |
| A | HIS206 |
| A | TRP245 |
| A | HOH503 |
| A | HOH533 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 402 |
| Chain | Residue |
| A | GLN211 |
| A | HOH526 |
| A | HOH532 |
| A | VAL209 |
| A | TYR210 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | binding site for residue PLP A 403 |
| Chain | Residue |
| A | GLY99 |
| A | SER100 |
| A | SER101 |
| A | TYR125 |
| A | ASN174 |
| A | ASP202 |
| A | TYR205 |
| A | SER231 |
| A | SER233 |
| A | LYS234 |
| A | ARG242 |
| B | TYR64 |
| B | ILE265 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue GOL B 402 |
| Chain | Residue |
| B | ARG307 |
| B | GLU375 |
| B | LEU378 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | binding site for residue AKG B 403 |
| Chain | Residue |
| B | ASP80 |
| B | TYR81 |
| B | HIS85 |
| B | GLU203 |
| B | HIS206 |
| B | THR216 |
| B | GLN221 |
| B | ASN230 |
| B | HOH547 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue GOL C 401 |
| Chain | Residue |
| C | ALA51 |
| C | ALA52 |
| C | HOH505 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue AKG C 402 |
| Chain | Residue |
| C | ASP80 |
| C | TYR81 |
| C | ARG84 |
| C | HIS85 |
| C | HIS206 |
| C | ASN230 |
| C | HOH511 |
| site_id | AC8 |
| Number of Residues | 20 |
| Details | binding site for Di-peptide PLP B 401 and LYS B 234 |
| Chain | Residue |
| A | TYR64 |
| A | ILE265 |
| B | GLY39 |
| B | PRO41 |
| B | GLY99 |
| B | SER100 |
| B | SER101 |
| B | TYR125 |
| B | TYR128 |
| B | ASN174 |
| B | ASP202 |
| B | TYR205 |
| B | SER231 |
| B | PHE232 |
| B | SER233 |
| B | TYR235 |
| B | TYR236 |
| B | ALA237 |
| B | ARG242 |
| B | HOH517 |
| site_id | AC9 |
| Number of Residues | 19 |
| Details | binding site for Di-peptide PLP C 403 and LYS C 234 |
| Chain | Residue |
| C | GLY39 |
| C | PRO41 |
| C | GLY99 |
| C | SER100 |
| C | SER101 |
| C | TYR125 |
| C | TYR128 |
| C | ASN174 |
| C | ASP202 |
| C | TYR205 |
| C | SER231 |
| C | PHE232 |
| C | SER233 |
| C | TYR235 |
| C | TYR236 |
| C | ALA237 |
| C | ARG242 |
| D | TYR64 |
| D | ILE265 |
| site_id | AD1 |
| Number of Residues | 17 |
| Details | binding site for Di-peptide PLP D 401 and LYS D 234 |
| Chain | Residue |
| D | TYR235 |
| D | TYR236 |
| D | ALA237 |
| D | ARG242 |
| C | TYR64 |
| C | ILE265 |
| D | GLY39 |
| D | PRO41 |
| D | SER100 |
| D | SER101 |
| D | TYR125 |
| D | ASN174 |
| D | ASP202 |
| D | TYR205 |
| D | SER231 |
| D | PHE232 |
| D | SER233 |
Functional Information from PROSITE/UniProt
| site_id | PS00105 |
| Number of Residues | 14 |
| Details | AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SFSKyyAMtGWRLG |
| Chain | Residue | Details |
| A | SER231-GLY244 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|Ref.5 |
| Chain | Residue | Details |
| A | LYS234 | |
| B | LYS234 | |
| C | LYS234 | |
| D | LYS234 |
