7NLN
Crystal structure of Mycobacterium tuberculosis ArgB in complex with N-acetyl-glutamate
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | arginine biosynthetic process |
A | 0009274 | cellular_component | peptidoglycan-based cell wall |
A | 0016301 | molecular_function | kinase activity |
A | 0042450 | biological_process | arginine biosynthetic process via ornithine |
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 | arginine biosynthetic process |
B | 0009274 | cellular_component | peptidoglycan-based cell wall |
B | 0016301 | molecular_function | kinase activity |
B | 0042450 | biological_process | 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: BINDING => ECO:0000255|HAMAP-Rule:MF_00082 |
Chain | Residue | Details |
A | GLY69 | |
A | ARG91 | |
A | ASN190 | |
B | GLY69 | |
B | ARG91 | |
B | ASN190 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | SITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_00082 |
Chain | Residue | Details |
A | LYS34 | |
A | LYS251 | |
B | LYS34 | |
B | LYS251 |