1PS8
Crystal Structure of the R270K Mutant of Aspartate Semialdehyde dehydrogenase from Haemophilus influenzae
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004073 | molecular_function | aspartate-semialdehyde dehydrogenase activity |
A | 0008652 | biological_process | amino acid biosynthetic process |
A | 0009085 | biological_process | lysine biosynthetic process |
A | 0009086 | biological_process | methionine biosynthetic process |
A | 0009088 | biological_process | threonine biosynthetic process |
A | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
A | 0009097 | biological_process | isoleucine 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 | 0019877 | biological_process | diaminopimelate biosynthetic process |
A | 0046983 | molecular_function | protein dimerization activity |
A | 0050661 | molecular_function | NADP binding |
A | 0051287 | molecular_function | NAD binding |
A | 0071266 | biological_process | 'de novo' L-methionine biosynthetic process |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Acyl-thioester intermediate => ECO:0000269|PubMed:14559965, ECO:0000269|PubMed:15272161 |
Chain | Residue | Details |
A | CYS136 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:14559965 |
Chain | Residue | Details |
A | HIS277 |
site_id | SWS_FT_FI3 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15272161 |
Chain | Residue | Details |
A | ARG10 | |
A | THR37 | |
A | GLN74 | |
A | SER166 | |
A | GLN353 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:14559965 |
Chain | Residue | Details |
A | ARG103 | |
A | LYS246 |
site_id | SWS_FT_FI5 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000305|PubMed:15272161 |
Chain | Residue | Details |
A | GLN163 | |
A | GLU243 | |
A | LYS270 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1brm |
Chain | Residue | Details |
A | CYS136 | |
A | HIS277 | |
A | GLN163 |