2WXB
Acetylglutamate kinase from Escherichia coli free of substrates
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003991 | molecular_function | acetylglutamate kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006526 | biological_process | L-arginine biosynthetic process |
| A | 0006974 | biological_process | DNA damage response |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0042450 | biological_process | L-arginine biosynthetic process via ornithine |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003991 | molecular_function | acetylglutamate kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006526 | biological_process | L-arginine biosynthetic process |
| B | 0006974 | biological_process | DNA damage response |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0042450 | biological_process | L-arginine biosynthetic process via ornithine |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE DTU A 1259 |
| Chain | Residue |
| A | LYS8 |
| A | GLY11 |
| A | VAL12 |
| A | GLY45 |
| A | HOH2067 |
| A | HOH2089 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT A 1260 |
| Chain | Residue |
| A | ASN160 |
| A | HOH2017 |
| A | HOH2028 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE DTU B 1259 |
| Chain | Residue |
| B | LYS8 |
| B | GLY10 |
| B | GLY11 |
| B | GLY45 |
| B | SER180 |
| B | HOH2005 |
| B | HOH2006 |
| B | HOH2087 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 1260 |
| Chain | Residue |
| A | SER135 |
| A | LEU136 |
| A | ASN139 |
| B | SER135 |
| B | ASN139 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00082","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12005432","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12875848","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00082","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12875848","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_00082","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12875848","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 870 |
| Chain | Residue | Details |
| A | LYS8 | transition state stabiliser |
| A | GLY11 | transition state stabiliser |
| A | GLY45 | transition state stabiliser |
| A | ASP162 | activator, steric role |
| A | LYS217 | transition state stabiliser |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 870 |
| Chain | Residue | Details |
| B | LYS8 | transition state stabiliser |
| B | GLY11 | transition state stabiliser |
| B | GLY45 | transition state stabiliser |
| B | ASP162 | activator, steric role |
| B | LYS217 | transition state stabiliser |
