1WOG
Crystal Structure of Agmatinase Reveals Structural Conservation and Inhibition Mechanism of the Ureohydrolase Superfamily
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 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 | 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 |
| D | 0008783 | molecular_function | agmatinase activity |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| D | 0033389 | biological_process | putrescine biosynthetic process from arginine, using agmatinase |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0008783 | molecular_function | agmatinase activity |
| E | 0016787 | molecular_function | hydrolase activity |
| E | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| E | 0033389 | biological_process | putrescine biosynthetic process from arginine, using agmatinase |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0008783 | molecular_function | agmatinase activity |
| F | 0016787 | molecular_function | hydrolase activity |
| F | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| F | 0033389 | biological_process | putrescine biosynthetic process from arginine, using agmatinase |
| F | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN A 1601 |
| Chain | Residue |
| A | HIS121 |
| A | ASP143 |
| A | ASP147 |
| A | ASP229 |
| A | 16D1401 |
| A | MN1602 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN A 1602 |
| Chain | Residue |
| A | ASP231 |
| A | 16D1401 |
| A | MN1601 |
| A | ASP143 |
| A | HIS145 |
| A | ASP229 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN B 1603 |
| Chain | Residue |
| B | HIS121 |
| B | ASP143 |
| B | ASP147 |
| B | ASP229 |
| B | 16D1402 |
| B | MN1604 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN B 1604 |
| Chain | Residue |
| B | ASP143 |
| B | HIS145 |
| B | ASP229 |
| B | ASP231 |
| B | 16D1402 |
| B | MN1603 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN C 1605 |
| Chain | Residue |
| C | HIS121 |
| C | ASP143 |
| C | ASP147 |
| C | ASP229 |
| C | 16D1403 |
| C | MN1606 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN C 1606 |
| Chain | Residue |
| C | ASP143 |
| C | HIS145 |
| C | ASP229 |
| C | ASP231 |
| C | 16D1403 |
| C | MN1605 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN D 1607 |
| Chain | Residue |
| D | HIS121 |
| D | ASP143 |
| D | ASP147 |
| D | ASP229 |
| D | 16D1404 |
| D | MN1608 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN D 1608 |
| Chain | Residue |
| D | ASP143 |
| D | HIS145 |
| D | ASP229 |
| D | ASP231 |
| D | 16D1404 |
| D | MN1607 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN E 1609 |
| Chain | Residue |
| E | HIS121 |
| E | ASP143 |
| E | ASP147 |
| E | ASP229 |
| E | 16D1405 |
| E | MN1610 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN E 1610 |
| Chain | Residue |
| E | ASP143 |
| E | HIS145 |
| E | ASP229 |
| E | ASP231 |
| E | 16D1405 |
| E | MN1609 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN F 1611 |
| Chain | Residue |
| F | HIS121 |
| F | ASP143 |
| F | ASP147 |
| F | ASP229 |
| F | 16D1406 |
| F | MN1612 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN F 1612 |
| Chain | Residue |
| F | ASP143 |
| F | HIS145 |
| F | ASP229 |
| F | ASP231 |
| F | 16D1406 |
| F | MN1611 |
| site_id | BC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE 16D A 1401 |
| Chain | Residue |
| A | HIS145 |
| A | ASP147 |
| A | ASN159 |
| A | SER160 |
| A | ASP229 |
| A | ASP231 |
| A | MN1601 |
| A | MN1602 |
| A | HOH1620 |
| A | HOH1672 |
| A | HOH1680 |
| site_id | BC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE 16D B 1402 |
| Chain | Residue |
| B | HIS145 |
| B | ASP147 |
| B | ASN159 |
| B | SER160 |
| B | ASP229 |
| B | ASP231 |
| B | MN1603 |
| B | MN1604 |
| B | HOH1605 |
| B | HOH1636 |
| B | HOH1723 |
| site_id | BC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE 16D C 1403 |
| Chain | Residue |
| C | ASP231 |
| C | MN1605 |
| C | MN1606 |
| C | HOH1629 |
| C | HOH1686 |
| C | HOH1712 |
| C | HIS145 |
| C | ASP147 |
| C | ASN159 |
| C | SER160 |
| C | ASP229 |
| site_id | BC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE 16D D 1404 |
| Chain | Residue |
| D | HIS145 |
| D | ASP147 |
| D | ASN159 |
| D | SER160 |
| D | ASP229 |
| D | ASP231 |
| D | MN1607 |
| D | MN1608 |
| D | HOH1611 |
| D | HOH1654 |
| D | HOH1675 |
| site_id | BC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE 16D E 1405 |
| Chain | Residue |
| E | HIS145 |
| E | ASP147 |
| E | ASN159 |
| E | SER160 |
| E | ASP229 |
| E | ASP231 |
| E | MN1609 |
| E | MN1610 |
| E | HOH1679 |
| E | HOH1689 |
| site_id | BC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE 16D F 1406 |
| Chain | Residue |
| F | HIS145 |
| F | ASP147 |
| F | ASN159 |
| F | SER160 |
| F | ASP229 |
| F | ASP231 |
| F | MN1611 |
| F | MN1612 |
| F | HOH1654 |
| F | HOH1670 |
Functional Information from PROSITE/UniProt
| site_id | PS01053 |
| Number of Residues | 22 |
| Details | ARGINASE_1 Arginase family signature. SVDVDgfdPaviPGtsspepdG |
| Chain | Residue | Details |
| A | SER227-GLY248 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cev |
| Chain | Residue | Details |
| A | GLU274 | |
| A | ASP147 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cev |
| Chain | Residue | Details |
| B | GLU274 | |
| B | ASP147 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cev |
| Chain | Residue | Details |
| C | GLU274 | |
| C | ASP147 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cev |
| Chain | Residue | Details |
| D | GLU274 | |
| D | ASP147 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cev |
| Chain | Residue | Details |
| E | GLU274 | |
| E | ASP147 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cev |
| Chain | Residue | Details |
| F | GLU274 | |
| F | ASP147 |
