3M5D
Crystal structure of N-acetyl-L-ornithine transcarbamylase K302R mutant complexed with PALAO
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004585 | molecular_function | ornithine carbamoyltransferase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0006526 | biological_process | L-arginine biosynthetic process |
| A | 0006591 | biological_process | ornithine metabolic process |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0016597 | molecular_function | amino acid binding |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016743 | molecular_function | carboxyl- or carbamoyltransferase activity |
| A | 0019240 | biological_process | citrulline biosynthetic process |
| A | 0042450 | biological_process | L-arginine biosynthetic process via ornithine |
| A | 0043857 | molecular_function | N-acetylornithine carbamoyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PA9 A 345 |
| Chain | Residue |
| A | SER49 |
| A | ASN185 |
| A | LYS252 |
| A | CYS294 |
| A | LEU295 |
| A | ARG322 |
| A | HOH374 |
| A | HOH438 |
| A | MET50 |
| A | ARG51 |
| A | THR52 |
| A | TRP77 |
| A | GLU92 |
| A | ARG112 |
| A | GLU144 |
| A | HIS148 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 350 |
| Chain | Residue |
| A | PHE61 |
| A | PHE61 |
| A | PHE61 |
| A | HIS66 |
| A | HIS66 |
| A | HIS66 |
| A | HOH342 |
| A | HOH342 |
| A | HOH342 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 9 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"16741992","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17600144","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3KZM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3KZO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L02","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L04","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L05","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L06","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16741992","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17600144","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3KZM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3KZO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L02","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L04","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L05","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L06","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16741992","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3KZN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Site: {"description":"Key residue in conferring substrate specificity for N-acetyl-L-ornithine versus N-succinyl-L-ornithine","evidences":[{"source":"PubMed","id":"17600144","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"PubMed","id":"20695527","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
