5EVC
Crystal structure of putative aspartate racemase from Salmonella Typhimurium complexed with sulfate and potassium
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0006520 | biological_process | amino acid metabolic process |
A | 0006807 | biological_process | obsolete nitrogen compound metabolic process |
A | 0016597 | molecular_function | amino acid binding |
A | 0016743 | molecular_function | carboxyl- or carbamoyltransferase activity |
A | 0016853 | molecular_function | isomerase activity |
A | 0016855 | molecular_function | racemase and epimerase activity, acting on amino acids and derivatives |
A | 0036361 | molecular_function | racemase activity, acting on amino acids and derivatives |
A | 0046872 | molecular_function | metal ion binding |
A | 0047661 | molecular_function | amino-acid racemase activity |
B | 0006520 | biological_process | amino acid metabolic process |
B | 0006807 | biological_process | obsolete nitrogen compound metabolic process |
B | 0016597 | molecular_function | amino acid binding |
B | 0016743 | molecular_function | carboxyl- or carbamoyltransferase activity |
B | 0016853 | molecular_function | isomerase activity |
B | 0016855 | molecular_function | racemase and epimerase activity, acting on amino acids and derivatives |
B | 0036361 | molecular_function | racemase activity, acting on amino acids and derivatives |
B | 0046872 | molecular_function | metal ion binding |
B | 0047661 | molecular_function | amino-acid racemase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue K A 301 |
Chain | Residue |
A | MET11 |
A | THR194 |
A | GLU195 |
A | SO4302 |
A | HOH421 |
site_id | AC2 |
Number of Residues | 10 |
Details | binding site for residue SO4 A 302 |
Chain | Residue |
A | THR124 |
A | LYS163 |
A | K301 |
A | HOH413 |
A | HOH417 |
A | HOH482 |
A | MET11 |
A | ARG49 |
A | CYS83 |
A | THR85 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue K A 303 |
Chain | Residue |
A | VAL24 |
A | GLU25 |
A | ARG27 |
A | HOH480 |
A | HOH523 |
site_id | AC4 |
Number of Residues | 8 |
Details | binding site for residue GOL A 304 |
Chain | Residue |
A | ASP111 |
A | ARG220 |
A | HOH441 |
A | HOH451 |
B | HIS28 |
B | ALA29 |
B | SER30 |
B | GLN34 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue FMT A 305 |
Chain | Residue |
A | PRO113 |
A | SER115 |
A | ARG164 |
A | HOH401 |
B | CYS31 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue CL A 306 |
Chain | Residue |
A | SER59 |
A | TYR61 |
A | ARG62 |
B | HIS118 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue K B 301 |
Chain | Residue |
B | MET11 |
B | THR194 |
B | GLU195 |
B | SO4302 |
B | F303 |
site_id | AC8 |
Number of Residues | 10 |
Details | binding site for residue SO4 B 302 |
Chain | Residue |
B | MET11 |
B | ARG49 |
B | CYS83 |
B | THR85 |
B | THR124 |
B | LYS163 |
B | K301 |
B | HOH402 |
B | HOH406 |
B | HOH486 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue F B 303 |
Chain | Residue |
B | CYS83 |
B | ASN84 |
B | CYS193 |
B | THR194 |
B | K301 |
B | HOH402 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue GOL B 304 |
Chain | Residue |
A | ARG224 |
B | ARG27 |
B | GLN34 |
B | THR232 |
B | HOH434 |
site_id | AD2 |
Number of Residues | 5 |
Details | binding site for residue K B 305 |
Chain | Residue |
B | VAL24 |
B | GLU25 |
B | ARG27 |
B | HOH461 |
B | HOH515 |
Functional Information from PROSITE/UniProt