1WOI
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 1501 |
Chain | Residue |
A | HIS121 |
A | ASP143 |
A | ASP147 |
A | ASP229 |
A | MN1502 |
A | HOH1636 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN A 1502 |
Chain | Residue |
A | ASP231 |
A | MN1501 |
A | HOH1636 |
A | ASP143 |
A | HIS145 |
A | ASP229 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN B 1503 |
Chain | Residue |
B | HIS121 |
B | ASP143 |
B | ASP147 |
B | ASP229 |
B | MN1504 |
B | HOH1601 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN B 1504 |
Chain | Residue |
B | ASP143 |
B | HIS145 |
B | ASP229 |
B | ASP231 |
B | MN1503 |
B | HOH1601 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN C 1505 |
Chain | Residue |
C | HIS121 |
C | ASP143 |
C | ASP147 |
C | ASP229 |
C | MN1506 |
C | HOH1630 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN C 1506 |
Chain | Residue |
C | ASP143 |
C | HIS145 |
C | ASP229 |
C | ASP231 |
C | MN1505 |
C | HOH1630 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN D 1507 |
Chain | Residue |
D | HIS121 |
D | ASP143 |
D | ASP147 |
D | ASP229 |
D | MN1508 |
D | HOH1600 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN D 1508 |
Chain | Residue |
D | ASP143 |
D | HIS145 |
D | ASP229 |
D | ASP231 |
D | MN1507 |
D | HOH1600 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN E 1509 |
Chain | Residue |
E | HIS121 |
E | ASP143 |
E | ASP147 |
E | ASP229 |
E | MN1510 |
E | HOH1616 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN E 1510 |
Chain | Residue |
E | ASP143 |
E | HIS145 |
E | ASP229 |
E | ASP231 |
E | MN1509 |
E | HOH1616 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN F 1511 |
Chain | Residue |
F | HIS121 |
F | ASP143 |
F | ASP147 |
F | ASP229 |
F | MN1512 |
F | HOH1627 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN F 1512 |
Chain | Residue |
F | ASP143 |
F | HIS145 |
F | ASP229 |
F | ASP231 |
F | MN1511 |
F | HOH1627 |
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 |