7NLN
Crystal structure of Mycobacterium tuberculosis ArgB in complex with N-acetyl-glutamate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003991 | molecular_function | acetylglutamate kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006526 | biological_process | L-arginine biosynthetic process |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009274 | cellular_component | peptidoglycan-based cell wall |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0042450 | biological_process | L-arginine biosynthetic process via ornithine |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003991 | molecular_function | acetylglutamate kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006526 | biological_process | L-arginine biosynthetic process |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009274 | cellular_component | peptidoglycan-based cell wall |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0042450 | biological_process | L-arginine biosynthetic process via ornithine |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | binding site for residue NLG A 301 |
| Chain | Residue |
| A | GLY68 |
| A | HOH401 |
| A | HOH445 |
| A | HOH462 |
| A | GLY69 |
| A | GLY70 |
| A | ILE73 |
| A | PHE90 |
| A | ARG91 |
| A | VAL154 |
| A | ASN190 |
| A | ALA193 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 302 |
| Chain | Residue |
| A | LYS34 |
| A | GLY36 |
| A | GLY37 |
| A | LEU212 |
| A | LYS251 |
| A | HOH445 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 303 |
| Chain | Residue |
| A | ARG173 |
| B | ALA164 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | binding site for residue NLG B 301 |
| Chain | Residue |
| B | GLY68 |
| B | GLY69 |
| B | GLY70 |
| B | ILE73 |
| B | ARG91 |
| B | VAL154 |
| B | ASN190 |
| B | ALA193 |
| B | HOH407 |
| B | HOH423 |
| B | HOH443 |
| B | HOH449 |
| B | HOH461 |
| B | HOH525 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 302 |
| Chain | Residue |
| B | LYS34 |
| B | GLY36 |
| B | GLY37 |
| B | LEU212 |
| B | LYS251 |
| B | HOH461 |
| B | HOH490 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00082","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_00082","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
