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CRYSTAL STRUCTURE OF HUMAN ORNITHINE TRANSCARBAMOYLASE COMPLEXED WITH N-PHOSPHONACETYL-L-ORNITHINE
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000050 | biological_process | urea cycle |
A | 0001889 | biological_process | liver development |
A | 0004585 | molecular_function | ornithine carbamoyltransferase activity |
A | 0005543 | molecular_function | phospholipid binding |
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 | arginine biosynthetic process |
A | 0006591 | biological_process | ornithine metabolic process |
A | 0006593 | biological_process | ornithine catabolic process |
A | 0007494 | biological_process | midgut development |
A | 0009410 | biological_process | response to xenobiotic stimulus |
A | 0010043 | biological_process | response to zinc ion |
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 | 0031667 | biological_process | response to nutrient levels |
A | 0032868 | biological_process | response to insulin |
A | 0042301 | molecular_function | phosphate ion binding |
A | 0042450 | biological_process | arginine biosynthetic process via ornithine |
A | 0042802 | molecular_function | identical protein binding |
A | 0055081 | biological_process | monoatomic anion homeostasis |
A | 0070781 | biological_process | response to biotin |
A | 0097272 | biological_process | ammonium homeostasis |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE PAO A 355 |
Chain | Residue |
A | SER90 |
A | ASN199 |
A | ASP263 |
A | SER267 |
A | MET268 |
A | LEU304 |
A | ARG330 |
A | HOH381 |
A | HOH385 |
A | THR91 |
A | ARG92 |
A | THR93 |
A | HIS117 |
A | ARG141 |
A | LEU163 |
A | HIS168 |
A | ASN198 |
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 | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:10813810 |
Chain | Residue | Details |
A | CYS303 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10813810, ECO:0007744|PDB:1C9Y |
Chain | Residue | Details |
A | SER90 | |
A | ARG141 | |
A | HIS168 | |
A | GLN171 | |
A | CYS303 | |
A | ARG330 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000305|PubMed:10813810, ECO:0007744|PDB:1C9Y |
Chain | Residue | Details |
A | ASN199 | |
A | ASP263 | |
A | SER267 | |
A | MET268 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P11725 |
Chain | Residue | Details |
A | LYS70 | |
A | LYS88 | |
A | LYS144 | |
A | LYS221 | |
A | LYS231 | |
A | LYS238 | |
A | LYS292 | |
A | LYS307 |
site_id | SWS_FT_FI5 |
Number of Residues | 3 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P11725 |
Chain | Residue | Details |
A | LYS80 | |
A | LYS274 | |
A | LYS289 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER133 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P11725 |
Chain | Residue | Details |
A | LYS243 |
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 |