6Q1Q
A hypothetical aminotransferase from Mycobacterium tuberculosis, apo form
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0005829 | cellular_component | cytosol |
A | 0005886 | cellular_component | plasma membrane |
A | 0008360 | biological_process | regulation of cell shape |
A | 0008483 | molecular_function | transaminase activity |
A | 0008696 | molecular_function | 4-amino-4-deoxychorismate lyase activity |
A | 0009252 | biological_process | peptidoglycan biosynthetic process |
A | 0016829 | molecular_function | lyase activity |
A | 0019752 | biological_process | carboxylic acid metabolic process |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
A | 0046394 | biological_process | carboxylic acid biosynthetic process |
A | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
A | 0046656 | biological_process | folic acid biosynthetic process |
B | 0003824 | molecular_function | catalytic activity |
B | 0005829 | cellular_component | cytosol |
B | 0005886 | cellular_component | plasma membrane |
B | 0008360 | biological_process | regulation of cell shape |
B | 0008483 | molecular_function | transaminase activity |
B | 0008696 | molecular_function | 4-amino-4-deoxychorismate lyase activity |
B | 0009252 | biological_process | peptidoglycan biosynthetic process |
B | 0016829 | molecular_function | lyase activity |
B | 0019752 | biological_process | carboxylic acid metabolic process |
B | 0030170 | molecular_function | pyridoxal phosphate binding |
B | 0046394 | biological_process | carboxylic acid biosynthetic process |
B | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
B | 0046656 | biological_process | folic acid biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | binding site for residue CIT A 301 |
Chain | Residue |
A | PHE31 |
A | HOH409 |
A | HOH419 |
A | HOH496 |
B | ARG26 |
A | THR33 |
A | ARG90 |
A | ARG115 |
A | ARG185 |
A | SER252 |
A | MET254 |
A | THR255 |
A | EDO305 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue CIT A 302 |
Chain | Residue |
A | LEU65 |
A | PRO66 |
A | ARG69 |
A | ARG238 |
A | HOH493 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue EDO A 303 |
Chain | Residue |
A | ARG37 |
A | ASP282 |
A | VAL286 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue EDO A 304 |
Chain | Residue |
A | TYR179 |
A | TYR210 |
A | ALA236 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue EDO A 305 |
Chain | Residue |
A | SER252 |
A | SER253 |
A | CIT301 |
A | HOH443 |
A | HOH445 |
A | HOH455 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue EDO B 301 |
Chain | Residue |
B | ALA148 |
B | LYS149 |
B | THR150 |
B | SER152 |
B | TYR153 |
B | HOH409 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000269|PubMed:33950161, ECO:0007744|PDB:6Q1R, ECO:0007744|PDB:6Q1S |
Chain | Residue | Details |
A | ARG50 | |
B | SER253 | |
A | TYR153 | |
A | THR216 | |
A | THR217 | |
A | SER253 | |
B | ARG50 | |
B | TYR153 | |
B | THR216 | |
B | THR217 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:33950161, ECO:0007744|PDB:6Q1S |
Chain | Residue | Details |
A | SER252 | |
A | MET254 | |
A | THR255 | |
B | SER252 | |
B | MET254 | |
B | THR255 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | SITE: Important for dual ACDL/DAAT activities => ECO:0000305|PubMed:33950161 |
Chain | Residue | Details |
A | ARG26 | |
B | ARG26 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:33950161, ECO:0007744|PDB:6Q1R |
Chain | Residue | Details |
A | LYS149 | |
B | LYS149 |