2I3G
Crystal structure of N-Acetyl-gamma-Glutamyl-Phosphate Reductase (Rv1652) from Mycobacterium tuberculosis in complex with NADP+.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003942 | molecular_function | N-acetyl-gamma-glutamyl-phosphate reductase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006526 | biological_process | L-arginine biosynthetic process |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| A | 0051287 | molecular_function | NAD binding |
| A | 0070401 | molecular_function | NADP+ binding |
| B | 0003942 | molecular_function | N-acetyl-gamma-glutamyl-phosphate reductase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006526 | biological_process | L-arginine biosynthetic process |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| B | 0051287 | molecular_function | NAD binding |
| B | 0070401 | molecular_function | NADP+ binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAP A 500 |
| Chain | Residue |
| A | GLY16 |
| A | THR73 |
| A | ALA87 |
| A | LEU88 |
| A | PRO89 |
| A | HIS90 |
| A | HIS92 |
| A | CYS109 |
| A | GLY110 |
| A | SER189 |
| A | GLY190 |
| A | SER18 |
| A | GLY192 |
| A | ARG193 |
| A | ALA194 |
| A | ASN320 |
| A | LEU321 |
| A | THR325 |
| A | HOH755 |
| A | HOH839 |
| A | HOH840 |
| A | HOH841 |
| A | GLY19 |
| A | HOH844 |
| A | HOH864 |
| A | HOH865 |
| A | HOH870 |
| A | TYR20 |
| A | ALA21 |
| A | ALA47 |
| A | ALA48 |
| A | THR49 |
| A | SER50 |
| site_id | AC2 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE NAP B 500 |
| Chain | Residue |
| B | GLY16 |
| B | SER18 |
| B | GLY19 |
| B | TYR20 |
| B | ALA21 |
| B | ALA47 |
| B | ALA48 |
| B | THR49 |
| B | SER50 |
| B | THR73 |
| B | ALA87 |
| B | LEU88 |
| B | PRO89 |
| B | HIS92 |
| B | CYS109 |
| B | GLY110 |
| B | SER189 |
| B | GLY190 |
| B | GLY192 |
| B | ARG193 |
| B | ALA194 |
| B | ASN320 |
| B | LEU321 |
| B | THR325 |
| B | HOH778 |
| B | HOH842 |
| B | HOH878 |
| B | HOH880 |
| B | HOH881 |
| B | HOH882 |
| B | HOH883 |
| B | HOH884 |
| B | HOH888 |
| B | HOH907 |
| B | HOH910 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BTB A 600 |
| Chain | Residue |
| A | HIS32 |
| A | ALA34 |
| A | ASP37 |
| A | ARG39 |
| A | TRP339 |
| A | PRO340 |
| A | ASP343 |
| A | HOH921 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BTB B 700 |
| Chain | Residue |
| B | HIS32 |
| B | ALA34 |
| B | ASP37 |
| B | ARG39 |
| B | TRP339 |
| B | PRO340 |
| B | ASP343 |
| B | HOH972 |
Functional Information from PROSITE/UniProt
| site_id | PS01224 |
| Number of Residues | 17 |
| Details | ARGC N-acetyl-gamma-glutamyl-phosphate reductase active site. IAvPGCYPTAallALfP |
| Chain | Residue | Details |
| A | ILE153-PRO169 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00150","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
