4JQO
Crystal structure of anabolic ornithine carbamoyltransferase from Vibrio vulnificus in complex with citrulline and inorganic phosphate
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 |
| B | 0004585 | molecular_function | ornithine carbamoyltransferase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0006526 | biological_process | L-arginine biosynthetic process |
| B | 0006591 | biological_process | ornithine metabolic process |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0016597 | molecular_function | amino acid binding |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016743 | molecular_function | carboxyl- or carbamoyltransferase activity |
| B | 0019240 | biological_process | citrulline biosynthetic process |
| B | 0042450 | biological_process | L-arginine biosynthetic process via ornithine |
| C | 0004585 | molecular_function | ornithine carbamoyltransferase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006520 | biological_process | amino acid metabolic process |
| C | 0006526 | biological_process | L-arginine biosynthetic process |
| C | 0006591 | biological_process | ornithine metabolic process |
| C | 0008652 | biological_process | amino acid biosynthetic process |
| C | 0016597 | molecular_function | amino acid binding |
| C | 0016740 | molecular_function | transferase activity |
| C | 0016743 | molecular_function | carboxyl- or carbamoyltransferase activity |
| C | 0019240 | biological_process | citrulline biosynthetic process |
| C | 0042450 | biological_process | L-arginine biosynthetic process via ornithine |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 A 401 |
| Chain | Residue |
| A | SER57 |
| A | THR58 |
| A | ARG59 |
| A | THR60 |
| A | ARG108 |
| A | CIR402 |
| B | GLN84 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE CIR A 402 |
| Chain | Residue |
| A | HIS135 |
| A | GLN138 |
| A | ASN169 |
| A | ASP233 |
| A | SER237 |
| A | MET238 |
| A | CYS275 |
| A | LEU276 |
| A | ARG320 |
| A | PO4401 |
| A | HOH598 |
| B | HOH619 |
| A | THR60 |
| A | ARG108 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 403 |
| Chain | Residue |
| A | LEU13 |
| A | PHE134 |
| A | PRO136 |
| A | SER173 |
| A | HOH510 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG A 404 |
| Chain | Residue |
| A | LEU262 |
| A | ASN267 |
| A | PRO268 |
| A | HOH654 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PEG A 405 |
| Chain | Residue |
| A | GLY295 |
| A | HOH569 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PEG A 406 |
| Chain | Residue |
| A | ARG167 |
| A | ALA192 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 B 401 |
| Chain | Residue |
| B | SER57 |
| B | THR58 |
| B | ARG59 |
| B | THR60 |
| B | ARG108 |
| B | CIR402 |
| C | GLN84 |
| site_id | AC8 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE CIR B 402 |
| Chain | Residue |
| B | THR60 |
| B | ARG108 |
| B | HIS135 |
| B | GLN138 |
| B | ASN169 |
| B | ASP233 |
| B | SER237 |
| B | MET238 |
| B | CYS275 |
| B | LEU276 |
| B | ARG320 |
| B | PO4401 |
| B | HOH523 |
| C | HOH515 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL B 403 |
| Chain | Residue |
| B | LEU13 |
| B | PHE134 |
| B | PRO136 |
| B | SER173 |
| B | HOH522 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG B 404 |
| Chain | Residue |
| B | LEU262 |
| B | ASN267 |
| B | PRO268 |
| B | HIS310 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PEG B 405 |
| Chain | Residue |
| A | GLU307 |
| B | HOH622 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 C 401 |
| Chain | Residue |
| A | GLN84 |
| C | SER57 |
| C | THR58 |
| C | ARG59 |
| C | THR60 |
| C | ARG108 |
| C | CIR402 |
| site_id | BC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE CIR C 402 |
| Chain | Residue |
| C | THR60 |
| C | ARG108 |
| C | LEU130 |
| C | HIS135 |
| C | GLN138 |
| C | ASN169 |
| C | ASP233 |
| C | SER237 |
| C | MET238 |
| C | CYS275 |
| C | LEU276 |
| C | ARG320 |
| C | PO4401 |
| C | HOH520 |
| C | HOH537 |
| site_id | BC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL C 403 |
| Chain | Residue |
| C | LEU13 |
| C | SER173 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG C 404 |
| Chain | Residue |
| C | LEU262 |
| C | LYS263 |
| C | ASN267 |
| C | HIS310 |
| site_id | BC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PEG C 405 |
| Chain | Residue |
| C | LYS213 |
| C | THR215 |
Functional Information from PROSITE/UniProt
| site_id | PS00097 |
| Number of Residues | 8 |
| Details | CARBAMOYLTRANSFERASE Aspartate and ornithine carbamoyltransferases signature. FeKaSTRT |
| Chain | Residue | Details |
| A | PHE53-THR60 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2012","submissionDatabase":"PDB data bank","title":"Structural studies of ornithine carbamoyltransferase from various pathogens.","authors":["Shabalin I.G.","Winsor J.","Grimshaw S.","Osinski T.","Chordia M.D.","Anderson W.F.","Minor W."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2013","submissionDatabase":"PDB data bank","title":"Crystal structures and kinetic properties of anabolic ornithine carbamoyltransferase from human pathogens Vibrio vulnificus and Bacillus anthracis.","authors":["Shabalin I.G.","Winsor J.","Grimshaw S.","Minor W."]}},{"source":"PDB","id":"4H31","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JFR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JHX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JQO","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2012","submissionDatabase":"PDB data bank","title":"Structural studies of ornithine carbamoyltransferase from various pathogens.","authors":["Shabalin I.G.","Winsor J.","Grimshaw S.","Osinski T.","Chordia M.D.","Anderson W.F.","Minor W."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2013","submissionDatabase":"PDB data bank","title":"Crystal structures and kinetic properties of anabolic ornithine carbamoyltransferase from human pathogens Vibrio vulnificus and Bacillus anthracis.","authors":["Shabalin I.G.","Winsor J.","Grimshaw S.","Minor W."]}},{"source":"PDB","id":"4H31","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JQO","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2012","submissionDatabase":"PDB data bank","title":"Structural studies of ornithine carbamoyltransferase from various pathogens.","authors":["Shabalin I.G.","Winsor J.","Grimshaw S.","Osinski T.","Chordia M.D.","Anderson W.F.","Minor W."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2013","submissionDatabase":"PDB data bank","title":"Crystal structures and kinetic properties of anabolic ornithine carbamoyltransferase from human pathogens Vibrio vulnificus and Bacillus anthracis.","authors":["Shabalin I.G.","Winsor J.","Grimshaw S.","Minor W."]}},{"source":"PDB","id":"4H31","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JHX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JQO","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |






