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 | 0006520 | biological_process | amino acid metabolic process |
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 | 0006520 | biological_process | amino acid metabolic process |
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 | 0006520 | biological_process | amino acid metabolic process |
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 | 0006520 | biological_process | amino acid metabolic process |
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 |