6Q1S
A hypothetical aminotransferase from Mycobacterium tuberculosis, alpha-ketoglutarate and PMP bound 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 |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0008360 | biological_process | regulation of cell shape |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0008696 | molecular_function | 4-amino-4-deoxychorismate lyase activity |
| C | 0009252 | biological_process | peptidoglycan biosynthetic process |
| C | 0016829 | molecular_function | lyase activity |
| C | 0019752 | biological_process | carboxylic acid metabolic process |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0046394 | biological_process | carboxylic acid biosynthetic process |
| C | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| C | 0046656 | biological_process | folic acid biosynthetic process |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0005829 | cellular_component | cytosol |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0008360 | biological_process | regulation of cell shape |
| D | 0008483 | molecular_function | transaminase activity |
| D | 0008696 | molecular_function | 4-amino-4-deoxychorismate lyase activity |
| D | 0009252 | biological_process | peptidoglycan biosynthetic process |
| D | 0016829 | molecular_function | lyase activity |
| D | 0019752 | biological_process | carboxylic acid metabolic process |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0046394 | biological_process | carboxylic acid biosynthetic process |
| D | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| D | 0046656 | biological_process | folic acid biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | binding site for residue PMP A 301 |
| Chain | Residue |
| A | ARG50 |
| A | GLY215 |
| A | THR216 |
| A | THR217 |
| A | SER252 |
| A | SER253 |
| A | AKG302 |
| A | HOH404 |
| A | HOH411 |
| A | HOH419 |
| A | HOH435 |
| A | TYR153 |
| A | GLU182 |
| A | GLY183 |
| A | PRO184 |
| A | ARG185 |
| A | SER186 |
| A | THR187 |
| A | LEU213 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | binding site for residue AKG A 302 |
| Chain | Residue |
| A | PHE31 |
| A | THR33 |
| A | ARG115 |
| A | LYS149 |
| A | SER252 |
| A | SER253 |
| A | MET254 |
| A | THR255 |
| A | PMP301 |
| A | HOH411 |
| B | ARG26 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | binding site for residue PMP B 301 |
| Chain | Residue |
| B | ARG50 |
| B | LYS149 |
| B | TYR153 |
| B | GLU182 |
| B | GLY183 |
| B | ARG185 |
| B | SER186 |
| B | THR187 |
| B | LEU213 |
| B | THR216 |
| B | THR217 |
| B | VAL251 |
| B | SER252 |
| B | SER253 |
| B | AKG302 |
| B | HOH442 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue AKG B 302 |
| Chain | Residue |
| A | ARG26 |
| B | ARG115 |
| B | MET157 |
| B | ARG185 |
| B | MET254 |
| B | THR255 |
| B | PMP301 |
| B | HOH402 |
| site_id | AC5 |
| Number of Residues | 17 |
| Details | binding site for residue PMP C 301 |
| Chain | Residue |
| C | ARG50 |
| C | LYS149 |
| C | TYR153 |
| C | GLU182 |
| C | PRO184 |
| C | ARG185 |
| C | SER186 |
| C | THR187 |
| C | LEU213 |
| C | GLY215 |
| C | THR216 |
| C | THR217 |
| C | SER252 |
| C | SER253 |
| C | AKG302 |
| C | HOH452 |
| C | HOH466 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue AKG C 302 |
| Chain | Residue |
| C | ARG115 |
| C | SER252 |
| C | MET254 |
| C | THR255 |
| C | PMP301 |
| C | HOH452 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue CIT C 303 |
| Chain | Residue |
| A | LEU65 |
| A | PRO66 |
| A | ARG69 |
| A | ARG238 |
| C | ARG121 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue CIT C 304 |
| Chain | Residue |
| A | ARG121 |
| C | LEU65 |
| C | ARG69 |
| C | ARG238 |
| site_id | AC9 |
| Number of Residues | 16 |
| Details | binding site for residue PMP D 301 |
| Chain | Residue |
| D | AKG302 |
| D | HOH403 |
| D | HOH417 |
| D | ARG50 |
| D | TYR153 |
| D | GLU182 |
| D | PRO184 |
| D | ARG185 |
| D | SER186 |
| D | THR187 |
| D | LEU213 |
| D | GLY215 |
| D | THR216 |
| D | THR217 |
| D | SER252 |
| D | SER253 |
| site_id | AD1 |
| Number of Residues | 8 |
| Details | binding site for residue AKG D 302 |
| Chain | Residue |
| C | ARG26 |
| D | THR33 |
| D | ARG115 |
| D | SER252 |
| D | MET254 |
| D | THR255 |
| D | PMP301 |
| D | HOH417 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:33950161, ECO:0007744|PDB:6Q1R, ECO:0007744|PDB:6Q1S |
| Chain | Residue | Details |
| A | ARG50 | |
| B | SER253 | |
| C | ARG50 | |
| C | TYR153 | |
| C | THR216 | |
| C | THR217 | |
| C | SER253 | |
| D | ARG50 | |
| D | TYR153 | |
| D | THR216 | |
| D | THR217 | |
| A | TYR153 | |
| D | SER253 | |
| A | THR216 | |
| A | THR217 | |
| A | SER253 | |
| B | ARG50 | |
| B | TYR153 | |
| B | THR216 | |
| B | THR217 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:33950161, ECO:0007744|PDB:6Q1S |
| Chain | Residue | Details |
| A | SER252 | |
| D | SER252 | |
| D | MET254 | |
| D | THR255 | |
| A | MET254 | |
| A | THR255 | |
| B | SER252 | |
| B | MET254 | |
| B | THR255 | |
| C | SER252 | |
| C | MET254 | |
| C | THR255 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | SITE: Important for dual ACDL/DAAT activities => ECO:0000305|PubMed:33950161 |
| Chain | Residue | Details |
| A | ARG26 | |
| B | ARG26 | |
| C | ARG26 | |
| D | ARG26 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:33950161, ECO:0007744|PDB:6Q1R |
| Chain | Residue | Details |
| A | LYS149 | |
| B | LYS149 | |
| C | LYS149 | |
| D | LYS149 |
