3WWM
Crystal structure of LysZ from Thermus thermophilus with ADP
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 | 0006526 | biological_process | arginine biosynthetic process |
A | 0009085 | biological_process | lysine biosynthetic process |
A | 0016301 | molecular_function | kinase activity |
A | 0019878 | biological_process | lysine biosynthetic process via aminoadipic acid |
A | 0043744 | molecular_function | N2-acetyl-L-aminoadipate kinase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE ADP A 301 |
Chain | Residue |
A | LYS5 |
A | ARG230 |
A | HOH401 |
A | HOH427 |
A | GLY7 |
A | GLY8 |
A | GLY36 |
A | GLY37 |
A | SER38 |
A | TYR78 |
A | TYR200 |
A | MET228 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000305|PubMed:25392000, ECO:0007744|PDB:3WWM |
Chain | Residue | Details |
A | TYR78 | |
A | LYS5 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02082 |
Chain | Residue | Details |
A | ARG64 | |
A | ASN168 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | SITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_02082 |
Chain | Residue | Details |
A | LYS231 | |
A | LYS5 |