1FB5
LOW RESOLUTION STRUCTURE OF OVINE ORNITHINE TRANSCARBMOYLASE IN THE UNLIGANDED STATE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000050 | biological_process | urea cycle |
| A | 0004585 | molecular_function | ornithine carbamoyltransferase activity |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005743 | cellular_component | mitochondrial inner membrane |
| A | 0005759 | cellular_component | mitochondrial matrix |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NVA A 900 |
| Chain | Residue |
| A | SER133 |
| A | MET134 |
| A | ASP136 |
| A | LYS331 |
Functional Information from PROSITE/UniProt
| site_id | PS00097 |
| Number of Residues | 8 |
| Details | CARBAMOYLTRANSFERASE Aspartate and ornithine carbamoyltransferases signature. FeKrSTRT |
| Chain | Residue | Details |
| A | PHE86-THR93 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"evidences":[{"source":"UniProtKB","id":"P00480","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10813810","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1C9Y","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 15 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10813810","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1C9Y","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P11725","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P11725","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P00480","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P11725","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1akm |
| Chain | Residue | Details |
| A | ARG141 | |
| A | ASP263 | |
| A | ARG330 | |
| A | GLN171 | |
| A | CYS303 | |
| A | HIS168 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1akm |
| Chain | Residue | Details |
| A | ARG92 | |
| A | ARG141 | |
| A | THR93 | |
| A | HIS168 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 12 |
| Chain | Residue | Details |
| A | ARG141 | electrostatic stabiliser, hydrogen bond donor |
| A | HIS168 | electrostatic stabiliser, hydrogen bond donor |
| A | GLN171 | activator, hydrogen bond acceptor |
| A | ASP263 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | CYS303 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | ARG330 | electrostatic stabiliser, hydrogen bond donor |
