7NNQ
Crystal structure of Mycobacterium tuberculosis ArgC in complex with nicotinamide adenine dinucleotide phosphate (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 | arginine 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 | arginine 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 |
| C | 0003942 | molecular_function | N-acetyl-gamma-glutamyl-phosphate reductase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006526 | biological_process | arginine biosynthetic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| C | 0051287 | molecular_function | NAD binding |
| C | 0070401 | molecular_function | NADP+ binding |
| D | 0003942 | molecular_function | N-acetyl-gamma-glutamyl-phosphate reductase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006526 | biological_process | arginine biosynthetic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| D | 0051287 | molecular_function | NAD binding |
| D | 0070401 | molecular_function | NADP+ binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 36 |
| Details | binding site for residue NAP A 401 |
| Chain | Residue |
| A | GLY16 |
| A | THR73 |
| A | ALA87 |
| A | LEU88 |
| A | PRO89 |
| A | HIS92 |
| A | CYS109 |
| A | GLY110 |
| A | SER189 |
| A | GLY190 |
| A | GLY192 |
| A | SER18 |
| A | ARG193 |
| A | ALA194 |
| A | ASN320 |
| A | LEU321 |
| A | GLY324 |
| A | THR325 |
| A | HOH514 |
| A | HOH523 |
| A | HOH541 |
| A | HOH555 |
| A | GLY19 |
| A | HOH556 |
| A | HOH560 |
| A | HOH566 |
| A | HOH634 |
| A | HOH672 |
| A | HOH684 |
| A | HOH697 |
| A | TYR20 |
| A | ALA21 |
| A | ALA47 |
| A | ALA48 |
| A | THR49 |
| A | SER50 |
| site_id | AC2 |
| Number of Residues | 38 |
| Details | binding site for residue NAP B 401 |
| 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 | GLY324 |
| B | THR325 |
| B | HOH523 |
| B | HOH541 |
| B | HOH552 |
| B | HOH558 |
| B | HOH560 |
| B | HOH579 |
| B | HOH618 |
| B | HOH619 |
| B | HOH635 |
| B | HOH638 |
| B | HOH639 |
| B | HOH656 |
| B | HOH664 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue BTB B 402 |
| Chain | Residue |
| B | HIS32 |
| B | ALA34 |
| B | ASP37 |
| B | ARG39 |
| B | TRP339 |
| B | PRO340 |
| B | ASP343 |
| site_id | AC4 |
| Number of Residues | 34 |
| Details | binding site for residue NAP C 401 |
| Chain | Residue |
| C | GLY192 |
| C | ARG193 |
| C | ALA194 |
| C | ASN320 |
| C | LEU321 |
| C | GLY324 |
| C | THR325 |
| C | HOH513 |
| C | HOH586 |
| C | HOH591 |
| C | HOH596 |
| C | HOH609 |
| C | HOH619 |
| C | HOH624 |
| C | HOH651 |
| C | HOH658 |
| C | GLY16 |
| C | SER18 |
| C | GLY19 |
| C | TYR20 |
| C | ALA21 |
| C | ALA47 |
| C | ALA48 |
| C | THR49 |
| C | SER50 |
| C | THR73 |
| C | ALA87 |
| C | LEU88 |
| C | PRO89 |
| C | HIS92 |
| C | CYS109 |
| C | GLY110 |
| C | SER189 |
| C | GLY190 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue BTB C 402 |
| Chain | Residue |
| C | HIS32 |
| C | ALA34 |
| C | ASP37 |
| C | ARG39 |
| C | TRP339 |
| C | ASP343 |
| site_id | AC6 |
| Number of Residues | 36 |
| Details | binding site for residue NAP D 401 |
| Chain | Residue |
| D | GLY16 |
| D | SER18 |
| D | GLY19 |
| D | TYR20 |
| D | ALA21 |
| D | ALA47 |
| D | ALA48 |
| D | THR49 |
| D | SER50 |
| D | THR73 |
| D | ALA87 |
| D | LEU88 |
| D | PRO89 |
| D | HIS92 |
| D | CYS109 |
| D | GLY110 |
| D | ARG114 |
| D | CYS158 |
| D | SER189 |
| D | GLY190 |
| D | GLY192 |
| D | ARG193 |
| D | ALA194 |
| D | ASN320 |
| D | LEU321 |
| D | GLY324 |
| D | THR325 |
| D | HOH525 |
| D | HOH536 |
| D | HOH543 |
| D | HOH565 |
| D | HOH601 |
| D | HOH612 |
| D | HOH643 |
| D | HOH645 |
| D | HOH652 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue BTB D 402 |
| Chain | Residue |
| D | HIS32 |
| D | ALA34 |
| D | ASP37 |
| D | ARG39 |
| D | TRP339 |
| D | PRO340 |
| D | ASP343 |
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 | 4 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00150 |
| Chain | Residue | Details |
| A | CYS158 | |
| B | CYS158 | |
| C | CYS158 | |
| D | CYS158 |
