6NIC
Crystal Structure of Medicago truncatula Agmatine Iminohydrolase (Deiminase) in Complex with 6-aminohexanamide
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004668 | molecular_function | protein-arginine deiminase activity |
| A | 0006596 | biological_process | polyamine biosynthetic process |
| A | 0009446 | biological_process | putrescine biosynthetic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0033388 | biological_process | putrescine biosynthetic process from arginine |
| A | 0047632 | molecular_function | agmatine deiminase activity |
| B | 0004668 | molecular_function | protein-arginine deiminase activity |
| B | 0006596 | biological_process | polyamine biosynthetic process |
| B | 0009446 | biological_process | putrescine biosynthetic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0033388 | biological_process | putrescine biosynthetic process from arginine |
| B | 0047632 | molecular_function | agmatine deiminase activity |
| C | 0004668 | molecular_function | protein-arginine deiminase activity |
| C | 0006596 | biological_process | polyamine biosynthetic process |
| C | 0009446 | biological_process | putrescine biosynthetic process |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0033388 | biological_process | putrescine biosynthetic process from arginine |
| C | 0047632 | molecular_function | agmatine deiminase activity |
| D | 0004668 | molecular_function | protein-arginine deiminase activity |
| D | 0006596 | biological_process | polyamine biosynthetic process |
| D | 0009446 | biological_process | putrescine biosynthetic process |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0033388 | biological_process | putrescine biosynthetic process from arginine |
| D | 0047632 | molecular_function | agmatine deiminase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | binding site for residue PGE A 401 |
| Chain | Residue |
| A | LEU182 |
| A | ASN187 |
| A | LEU190 |
| A | SER191 |
| A | LYS192 |
| A | SER193 |
| A | HOH658 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue PGE A 402 |
| Chain | Residue |
| A | GLY319 |
| A | HIS345 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | binding site for residue KQY A 403 |
| Chain | Residue |
| A | ASP94 |
| A | TRP125 |
| A | GLY164 |
| A | ASP220 |
| A | THR221 |
| A | HIS224 |
| A | ASP226 |
| A | GLY361 |
| A | CYS366 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | binding site for residue PEG A 404 |
| Chain | Residue |
| A | GLN68 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue PEG A 405 |
| Chain | Residue |
| A | ARG151 |
| A | HOH533 |
| B | ASP78 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 406 |
| Chain | Residue |
| A | TRP125 |
| A | ASP130 |
| A | ASP219 |
| A | ASP220 |
| A | ASN222 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | binding site for residue PEG B 401 |
| Chain | Residue |
| B | TRP91 |
| B | ASP94 |
| B | CYS132 |
| B | ASP220 |
| B | THR221 |
| B | HIS224 |
| B | ARG301 |
| B | SER360 |
| B | GLY361 |
| B | CYS366 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue NA B 402 |
| Chain | Residue |
| B | TRP125 |
| B | ASP130 |
| B | ASP219 |
| B | ASP220 |
| B | ASN222 |
| B | HOH546 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue EDO C 401 |
| Chain | Residue |
| C | HOH644 |
| D | SER191 |
| D | LYS192 |
| D | SER193 |
| site_id | AD1 |
| Number of Residues | 8 |
| Details | binding site for residue KQY C 402 |
| Chain | Residue |
| C | ASP94 |
| C | TRP125 |
| C | HIS224 |
| C | ASP226 |
| C | GLY361 |
| C | CYS366 |
| C | HOH513 |
| C | HOH638 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue NA C 403 |
| Chain | Residue |
| C | TRP125 |
| C | ASP130 |
| C | ASP219 |
| C | ASP220 |
| C | ASN222 |
| C | HOH709 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue EDO D 401 |
| Chain | Residue |
| A | ARG206 |
| A | ALA266 |
| D | CYS134 |
| D | ASP135 |
| D | TRP136 |
| D | SER137 |
| site_id | AD4 |
| Number of Residues | 8 |
| Details | binding site for residue KQY D 402 |
| Chain | Residue |
| D | TRP91 |
| D | ASP94 |
| D | CYS132 |
| D | THR221 |
| D | HIS224 |
| D | ASP226 |
| D | CYS366 |
| D | HOH604 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue NA D 403 |
| Chain | Residue |
| D | TRP125 |
| D | ASP130 |
| D | ASP219 |
| D | ASP220 |
| D | ASN222 |
| D | HOH632 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Amidino-cysteine intermediate => ECO:0000250|UniProtKB:Q837U5 |
| Chain | Residue | Details |
| A | CYS366 | |
| B | CYS366 | |
| C | CYS366 | |
| D | CYS366 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:30984210, ECO:0007744|PDB:6NIC |
| Chain | Residue | Details |
| A | ASP220 | |
| A | ASP226 | |
| B | ASP220 | |
| B | ASP226 | |
| C | ASP220 | |
| C | ASP226 | |
| D | ASP220 | |
| D | ASP226 |
