3PZL
The crystal structure of agmatine ureohydrolase of Thermoplasma volcanium
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0008783 | molecular_function | agmatinase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| A | 0033389 | biological_process | putrescine biosynthetic process from arginine, using agmatinase |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0008783 | molecular_function | agmatinase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| B | 0033389 | biological_process | putrescine biosynthetic process from arginine, using agmatinase |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0008783 | molecular_function | agmatinase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| C | 0033389 | biological_process | putrescine biosynthetic process from arginine, using agmatinase |
| C | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 314 |
| Chain | Residue |
| A | HIS124 |
| A | ASP144 |
| A | ASP148 |
| A | ASP229 |
| A | MN315 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 315 |
| Chain | Residue |
| A | MN314 |
| A | ASP144 |
| A | HIS146 |
| A | ASP229 |
| A | ASP231 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN B 314 |
| Chain | Residue |
| B | HIS124 |
| B | ASP144 |
| B | ASP148 |
| B | ASP229 |
| B | MN315 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN B 315 |
| Chain | Residue |
| B | ASP144 |
| B | HIS146 |
| B | ASP148 |
| B | ASP229 |
| B | ASP231 |
| B | MN314 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN C 314 |
| Chain | Residue |
| C | ASP144 |
| C | HIS146 |
| C | ASP229 |
| C | ASP231 |
| C | MN315 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN C 315 |
| Chain | Residue |
| C | HIS124 |
| C | ASP144 |
| C | ASP148 |
| C | ASP229 |
| C | MN314 |
Functional Information from PROSITE/UniProt
| site_id | PS01053 |
| Number of Residues | 22 |
| Details | ARGINASE_1 Arginase family signature. SVDMDgidPayaPAvgtpepfG |
| Chain | Residue | Details |
| A | SER227-GLY248 |
