4E4J
Crystal structure of arginine deiminase from Mycoplasma penetrans
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006527 | biological_process | L-arginine catabolic process |
| A | 0016990 | molecular_function | arginine deiminase activity |
| B | 0006527 | biological_process | L-arginine catabolic process |
| B | 0016990 | molecular_function | arginine deiminase activity |
| C | 0006527 | biological_process | L-arginine catabolic process |
| C | 0016990 | molecular_function | arginine deiminase activity |
| D | 0006527 | biological_process | L-arginine catabolic process |
| D | 0016990 | molecular_function | arginine deiminase activity |
| E | 0006527 | biological_process | L-arginine catabolic process |
| E | 0016990 | molecular_function | arginine deiminase activity |
| F | 0006527 | biological_process | L-arginine catabolic process |
| F | 0016990 | molecular_function | arginine deiminase activity |
| G | 0006527 | biological_process | L-arginine catabolic process |
| G | 0016990 | molecular_function | arginine deiminase activity |
| H | 0006527 | biological_process | L-arginine catabolic process |
| H | 0016990 | molecular_function | arginine deiminase activity |
| I | 0006527 | biological_process | L-arginine catabolic process |
| I | 0016990 | molecular_function | arginine deiminase activity |
| J | 0006527 | biological_process | L-arginine catabolic process |
| J | 0016990 | molecular_function | arginine deiminase activity |
| K | 0006527 | biological_process | L-arginine catabolic process |
| K | 0016990 | molecular_function | arginine deiminase activity |
| L | 0006527 | biological_process | L-arginine catabolic process |
| L | 0016990 | molecular_function | arginine deiminase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 501 |
| Chain | Residue |
| A | GLU407 |
| A | ARG408 |
| A | GLY428 |
| B | LYS94 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 501 |
| Chain | Residue |
| A | LYS94 |
| B | GLU407 |
| B | ARG408 |
| B | GLY428 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL C 501 |
| Chain | Residue |
| C | GLY428 |
| D | LYS94 |
| C | ARG408 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL D 501 |
| Chain | Residue |
| C | LYS94 |
| D | ARG408 |
| D | GLY428 |
| D | SER429 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL E 501 |
| Chain | Residue |
| E | GLU407 |
| E | ARG408 |
| E | GLY428 |
| F | LYS94 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL F 501 |
| Chain | Residue |
| E | LYS94 |
| F | GLU407 |
| F | ARG408 |
| F | GLY428 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL G 501 |
| Chain | Residue |
| G | GLU407 |
| G | ARG408 |
| G | GLY428 |
| G | SER429 |
| H | LYS94 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL H 501 |
| Chain | Residue |
| G | LYS94 |
| H | GLU407 |
| H | ARG408 |
| H | GLY428 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL I 501 |
| Chain | Residue |
| I | GLU407 |
| I | ARG408 |
| I | GLY428 |
| I | SER429 |
| J | LYS94 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL J 501 |
| Chain | Residue |
| I | LYS94 |
| J | GLU407 |
| J | ARG408 |
| J | GLY428 |
| J | SER429 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL K 501 |
| Chain | Residue |
| K | GLU407 |
| K | ARG408 |
| K | GLY428 |
| L | LYS94 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL L 501 |
| Chain | Residue |
| K | LYS94 |
| L | GLU407 |
| L | ARG408 |
| L | GLY428 |
