1MDX
Crystal structure of ArnB transferase with pyridoxal 5' phosphate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000271 | biological_process | polysaccharide biosynthetic process |
A | 0006629 | biological_process | lipid metabolic process |
A | 0008483 | molecular_function | transaminase activity |
A | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
A | 0009245 | biological_process | lipid A biosynthetic process |
A | 0016020 | cellular_component | membrane |
A | 0016740 | molecular_function | transferase activity |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
A | 0046493 | biological_process | lipid A metabolic process |
A | 0046677 | biological_process | response to antibiotic |
A | 0099620 | molecular_function | UDP-4-amino-4-deoxy-L-arabinose aminotransferase |
Functional Information from PDB Data
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE AKG A 401 |
Chain | Residue |
A | THR36 |
A | HOH820 |
A | TRP89 |
A | HIS185 |
A | GLU194 |
A | PHE214 |
A | ARG229 |
A | LYS241 |
A | ASN243 |
A | HOH404 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 402 |
Chain | Residue |
A | SER61 |
A | SER61 |
A | GLU194 |
A | GLU194 |
A | LEU244 |
A | LEU244 |
A | PRO245 |
A | ASN248 |
A | ASN248 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 403 |
Chain | Residue |
A | PHE13 |
A | ARG229 |
A | GLY327 |
A | LEU328 |
A | HOH733 |
A | HOH820 |
A | HOH839 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"12429098","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"24460375","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"12429098","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1MDX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1MDZ","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1b9h |
Chain | Residue | Details |
A | ASP160 | |
A | TRP89 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1b9h |
Chain | Residue | Details |
A | ILE35 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1b9h |
Chain | Residue | Details |
A | ASP160 | |
A | LYS188 | |
A | TRP89 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1b9h |
Chain | Residue | Details |
A | ALA186 | |
A | ASP160 | |
A | TRP89 |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1b9h |
Chain | Residue | Details |
A | HIS163 | |
A | LYS188 |