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 |