5YU0
Structural basis for recognition of L-lysine, L-ornithine, and L-2,4-diamino butyric acid by lysine cyclodeaminase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0008473 | molecular_function | ornithine cyclodeaminase activity |
A | 0016829 | molecular_function | lyase activity |
B | 0000166 | molecular_function | nucleotide binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0008473 | molecular_function | ornithine cyclodeaminase activity |
B | 0016829 | molecular_function | lyase activity |
C | 0000166 | molecular_function | nucleotide binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0008473 | molecular_function | ornithine cyclodeaminase activity |
C | 0016829 | molecular_function | lyase activity |
D | 0000166 | molecular_function | nucleotide binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0008473 | molecular_function | ornithine cyclodeaminase activity |
D | 0016829 | molecular_function | lyase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue NA A 401 |
Chain | Residue |
A | ALA232 |
A | GLY234 |
A | GLY265 |
A | ASP300 |
A | SER301 |
site_id | AC2 |
Number of Residues | 34 |
Details | binding site for residue NAD A 402 |
Chain | Residue |
A | ARG121 |
A | THR122 |
A | GLY145 |
A | GLY147 |
A | ALA148 |
A | GLN149 |
A | ASP170 |
A | THR171 |
A | HIS175 |
A | THR209 |
A | SER210 |
A | VAL211 |
A | VAL218 |
A | VAL233 |
A | ALA235 |
A | ASP236 |
A | LYS240 |
A | SER301 |
A | THR302 |
A | GLY303 |
A | HOH532 |
A | HOH545 |
A | HOH557 |
A | HOH560 |
A | HOH585 |
A | HOH651 |
A | HOH655 |
A | HOH657 |
A | HOH726 |
B | LEU338 |
A | TYR81 |
A | THR93 |
A | ILE94 |
A | THR118 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue NA B 401 |
Chain | Residue |
B | ALA232 |
B | GLY234 |
B | GLY265 |
B | ASP300 |
B | SER301 |
site_id | AC4 |
Number of Residues | 33 |
Details | binding site for residue NAD B 402 |
Chain | Residue |
A | LEU338 |
B | TYR81 |
B | THR93 |
B | ILE94 |
B | ARG121 |
B | THR122 |
B | GLY147 |
B | ALA148 |
B | GLN149 |
B | ASP170 |
B | THR171 |
B | HIS175 |
B | ALA208 |
B | THR209 |
B | SER210 |
B | VAL211 |
B | VAL218 |
B | VAL233 |
B | GLY234 |
B | ALA235 |
B | ASP236 |
B | LYS240 |
B | SER301 |
B | THR302 |
B | GLY303 |
B | HOH536 |
B | HOH548 |
B | HOH555 |
B | HOH585 |
B | HOH614 |
B | HOH625 |
B | HOH666 |
B | HOH767 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue NA C 401 |
Chain | Residue |
C | ALA232 |
C | GLY234 |
C | GLY265 |
C | GLU266 |
C | ASP300 |
C | SER301 |
site_id | AC6 |
Number of Residues | 36 |
Details | binding site for residue NAD C 402 |
Chain | Residue |
C | VAL211 |
C | VAL233 |
C | GLY234 |
C | ALA235 |
C | ASP236 |
C | LYS240 |
C | SER301 |
C | THR302 |
C | GLY303 |
C | HOH514 |
C | HOH525 |
C | HOH574 |
C | HOH576 |
C | HOH592 |
C | HOH638 |
C | HOH649 |
C | HOH684 |
C | HOH722 |
C | HOH730 |
D | LEU338 |
C | TYR81 |
C | THR93 |
C | ILE94 |
C | THR118 |
C | ARG121 |
C | THR122 |
C | GLY145 |
C | GLY147 |
C | ALA148 |
C | GLN149 |
C | ASP170 |
C | THR171 |
C | HIS175 |
C | ALA208 |
C | THR209 |
C | SER210 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue NA D 401 |
Chain | Residue |
D | ALA232 |
D | GLY234 |
D | GLY265 |
D | GLU266 |
D | ASP300 |
D | SER301 |
site_id | AC8 |
Number of Residues | 36 |
Details | binding site for residue NAD D 402 |
Chain | Residue |
C | LEU338 |
D | TYR81 |
D | THR93 |
D | ILE94 |
D | THR118 |
D | ARG121 |
D | THR122 |
D | ILE144 |
D | GLY145 |
D | GLY147 |
D | ALA148 |
D | GLN149 |
D | ASP170 |
D | THR171 |
D | HIS175 |
D | ALA208 |
D | THR209 |
D | SER210 |
D | VAL211 |
D | VAL218 |
D | VAL233 |
D | ALA235 |
D | ASP236 |
D | LYS240 |
D | SER301 |
D | THR302 |
D | GLY303 |
D | HOH524 |
D | HOH530 |
D | HOH538 |
D | HOH556 |
D | HOH561 |
D | HOH612 |
D | HOH625 |
D | HOH672 |
D | HOH709 |