5EIO
Crystal structure of LysY from Thermus thermophilus complexed with NADP+ and LysW-gamma-aminoadipic semialdehyde
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003942 | molecular_function | N-acetyl-gamma-glutamyl-phosphate reductase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006526 | biological_process | arginine biosynthetic process |
| A | 0009085 | biological_process | lysine 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 | 0019878 | biological_process | lysine biosynthetic process via aminoadipic acid |
| A | 0043870 | molecular_function | N-acetyl-gamma-aminoadipyl-phosphate reductase activity |
| A | 0051287 | molecular_function | NAD binding |
| A | 0070401 | molecular_function | NADP+ binding |
| B | 0003942 | molecular_function | N-acetyl-gamma-glutamyl-phosphate reductase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006526 | biological_process | arginine biosynthetic process |
| B | 0009085 | biological_process | lysine 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 | 0019878 | biological_process | lysine biosynthetic process via aminoadipic acid |
| B | 0043870 | molecular_function | N-acetyl-gamma-aminoadipyl-phosphate reductase activity |
| B | 0051287 | molecular_function | NAD binding |
| B | 0070401 | molecular_function | NADP+ binding |
| C | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 32 |
| Details | binding site for residue NAP A 401 |
| Chain | Residue |
| A | GLY10 |
| A | ALA74 |
| A | LEU75 |
| A | PRO76 |
| A | HIS77 |
| A | VAL79 |
| A | LEU97 |
| A | SER98 |
| A | SER180 |
| A | ALA181 |
| A | GLY183 |
| A | ALA11 |
| A | ALA184 |
| A | ASN312 |
| A | LEU313 |
| A | THR317 |
| A | HOH505 |
| A | HOH521 |
| A | HOH536 |
| A | HOH549 |
| A | HOH559 |
| A | HOH563 |
| A | SER12 |
| A | HOH576 |
| A | HOH593 |
| A | HOH634 |
| A | GLY13 |
| A | TYR14 |
| A | ALA15 |
| A | SER36 |
| A | ARG37 |
| A | ARG38 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | binding site for residue ACY A 402 |
| Chain | Residue |
| A | HIS45 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue ACY A 403 |
| Chain | Residue |
| A | LYS4 |
| A | ASP69 |
| A | PRO92 |
| A | ILE93 |
| A | HOH604 |
| site_id | AC4 |
| Number of Residues | 36 |
| Details | binding site for residue NAP B 401 |
| Chain | Residue |
| B | GLY10 |
| B | ALA11 |
| B | SER12 |
| B | GLY13 |
| B | TYR14 |
| B | ALA15 |
| B | SER36 |
| B | ARG37 |
| B | ARG38 |
| B | ALA74 |
| B | LEU75 |
| B | PRO76 |
| B | HIS77 |
| B | VAL79 |
| B | LEU97 |
| B | SER98 |
| B | ARG102 |
| B | SER180 |
| B | ALA181 |
| B | GLY183 |
| B | ALA184 |
| B | ASN312 |
| B | LEU313 |
| B | THR317 |
| B | HOH507 |
| B | HOH517 |
| B | HOH520 |
| B | HOH537 |
| B | HOH538 |
| B | HOH549 |
| B | HOH553 |
| B | HOH569 |
| B | HOH580 |
| B | HOH589 |
| B | HOH602 |
| B | HOH617 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue ACY B 402 |
| Chain | Residue |
| A | ARG258 |
| B | PRO62 |
| B | ARG86 |
| B | TYR87 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue ACY B 403 |
| Chain | Residue |
| B | LYS167 |
| B | ASP246 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue ACY B 404 |
| Chain | Residue |
| B | GLU259 |
| B | ALA260 |
| B | ALA262 |
| B | GLU264 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue ZN C 101 |
| Chain | Residue |
| C | CYS5 |
| C | CYS8 |
| C | CYS25 |
| C | CYS28 |
Functional Information from PROSITE/UniProt
| site_id | PS01224 |
| Number of Residues | 17 |
| Details | ARGC N-acetyl-gamma-glutamyl-phosphate reductase active site. IAgAGCNATAtllGLyP |
| Chain | Residue | Details |
| A | ILE143-PRO159 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_02083, ECO:0000305|PubMed:26966182 |
| Chain | Residue | Details |
| A | CYS148 | |
| B | CYS148 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02083, ECO:0000269|PubMed:26966182 |
| Chain | Residue | Details |
| A | SER12 | |
| A | SER36 | |
| A | ASN312 | |
| B | SER12 | |
| B | SER36 | |
| B | ASN312 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:26966182 |
| Chain | Residue | Details |
| A | LEU75 | |
| A | SER180 | |
| A | ALA184 | |
| B | LEU75 | |
| B | SER180 | |
| B | ALA184 |
