1NR9
Crystal Structure of Escherichia coli 1262 (APC5008), Putative Isomerase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0006107 | biological_process | oxaloacetate metabolic process |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0018773 | molecular_function | acetylpyruvate hydrolase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050163 | molecular_function | oxaloacetate tautomerase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0006107 | biological_process | oxaloacetate metabolic process |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0018773 | molecular_function | acetylpyruvate hydrolase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050163 | molecular_function | oxaloacetate tautomerase activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0006107 | biological_process | oxaloacetate metabolic process |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0018773 | molecular_function | acetylpyruvate hydrolase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0050163 | molecular_function | oxaloacetate tautomerase activity |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0006107 | biological_process | oxaloacetate metabolic process |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0018773 | molecular_function | acetylpyruvate hydrolase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0050163 | molecular_function | oxaloacetate tautomerase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG A 301 |
| Chain | Residue |
| A | VAL22 |
| A | GLY23 |
| A | GLU70 |
| A | GLU72 |
| A | ASP101 |
| A | LYS122 |
| A | HOH334 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 302 |
| Chain | Residue |
| B | GLU70 |
| B | GLU72 |
| B | ASP101 |
| B | HOH310 |
| B | VAL22 |
| B | GLY23 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG C 303 |
| Chain | Residue |
| C | VAL22 |
| C | GLU70 |
| C | GLU72 |
| C | ASP101 |
| C | HOH308 |
| C | HOH344 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG D 304 |
| Chain | Residue |
| D | VAL22 |
| D | GLY23 |
| D | GLU70 |
| D | GLU72 |
| D | ASP101 |
| D | HOH366 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2003","submissionDatabase":"PDB data bank","title":"Crystal Structure of Escherichia coli Putative Isomerase EC1262 (APC5008).","authors":["Kim Y.","Joachimiak A.","Edwards A.","Skarina T.","Savchenko A."]}},{"source":"PDB","id":"1NR9","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
