1GQ7
PROCLAVAMINATE AMIDINO HYDROLASE FROM STREPTOMYCES CLAVULIGERUS
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 | 0033050 | biological_process | clavulanic acid biosynthetic process |
| A | 0033389 | biological_process | putrescine biosynthetic process from arginine, via agmatine |
| A | 0033972 | molecular_function | proclavaminate amidinohydrolase activity |
| 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 | 0033050 | biological_process | clavulanic acid biosynthetic process |
| B | 0033389 | biological_process | putrescine biosynthetic process from arginine, via agmatine |
| B | 0033972 | molecular_function | proclavaminate amidinohydrolase activity |
| 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 | 0033050 | biological_process | clavulanic acid biosynthetic process |
| C | 0033389 | biological_process | putrescine biosynthetic process from arginine, via agmatine |
| C | 0033972 | molecular_function | proclavaminate amidinohydrolase activity |
| 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 | 0033050 | biological_process | clavulanic acid biosynthetic process |
| D | 0033389 | biological_process | putrescine biosynthetic process from arginine, via agmatine |
| D | 0033972 | molecular_function | proclavaminate amidinohydrolase activity |
| 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 | 0033050 | biological_process | clavulanic acid biosynthetic process |
| E | 0033389 | biological_process | putrescine biosynthetic process from arginine, via agmatine |
| E | 0033972 | molecular_function | proclavaminate amidinohydrolase activity |
| 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 | 0033050 | biological_process | clavulanic acid biosynthetic process |
| F | 0033389 | biological_process | putrescine biosynthetic process from arginine, via agmatine |
| F | 0033972 | molecular_function | proclavaminate amidinohydrolase activity |
| F | 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 350 |
| Chain | Residue |
| A | HIS121 |
| A | ASP144 |
| A | ASP148 |
| A | ASP235 |
| A | MN351 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 351 |
| Chain | Residue |
| A | MN350 |
| A | ASP144 |
| A | HIS146 |
| A | ASP235 |
| A | ASP237 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN B 350 |
| Chain | Residue |
| B | HIS121 |
| B | ASP144 |
| B | ASP148 |
| B | ASP235 |
| B | MN351 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN B 351 |
| Chain | Residue |
| B | ASP144 |
| B | HIS146 |
| B | ASP235 |
| B | ASP237 |
| B | MN350 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN C 350 |
| Chain | Residue |
| C | HIS121 |
| C | ASP144 |
| C | ASP148 |
| C | ASP235 |
| C | MN351 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN C 351 |
| Chain | Residue |
| C | ASP144 |
| C | HIS146 |
| C | ASP235 |
| C | ASP237 |
| C | MN350 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN D 350 |
| Chain | Residue |
| D | HIS121 |
| D | ASP144 |
| D | ASP148 |
| D | ASP235 |
| D | MN351 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN D 351 |
| Chain | Residue |
| D | ASP144 |
| D | HIS146 |
| D | ASP235 |
| D | ASP237 |
| D | MN350 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN E 350 |
| Chain | Residue |
| E | HIS121 |
| E | ASP144 |
| E | ASP148 |
| E | ASP235 |
| E | MN351 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN E 351 |
| Chain | Residue |
| E | ASP144 |
| E | HIS146 |
| E | ASP235 |
| E | ASP237 |
| E | MN350 |
| E | HOH2076 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN F 350 |
| Chain | Residue |
| F | HIS121 |
| F | ASP144 |
| F | ASP148 |
| F | ASP235 |
| F | MN351 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN F 351 |
| Chain | Residue |
| F | ASP144 |
| F | HIS146 |
| F | ASP235 |
| F | ASP237 |
| F | MN350 |
Functional Information from PROSITE/UniProt
| site_id | PS01053 |
| Number of Residues | 22 |
| Details | ARGINASE_1 Arginase family signature. SVDIDvvdPafaPGtgtpapgG |
| Chain | Residue | Details |
| A | SER233-GLY254 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 36 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12020346, ECO:0007744|PDB:1GQ6, ECO:0007744|PDB:1GQ7 |
| Chain | Residue | Details |
| A | HIS121 | |
| B | ASP148 | |
| B | ASP235 | |
| B | ASP237 | |
| C | HIS121 | |
| C | ASP144 | |
| C | HIS146 | |
| C | ASP148 | |
| C | ASP235 | |
| C | ASP237 | |
| D | HIS121 | |
| A | ASP144 | |
| D | ASP144 | |
| D | HIS146 | |
| D | ASP148 | |
| D | ASP235 | |
| D | ASP237 | |
| E | HIS121 | |
| E | ASP144 | |
| E | HIS146 | |
| E | ASP148 | |
| E | ASP235 | |
| A | HIS146 | |
| E | ASP237 | |
| F | HIS121 | |
| F | ASP144 | |
| F | HIS146 | |
| F | ASP148 | |
| F | ASP235 | |
| F | ASP237 | |
| A | ASP148 | |
| A | ASP235 | |
| A | ASP237 | |
| B | HIS121 | |
| B | ASP144 | |
| B | HIS146 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cev |
| Chain | Residue | Details |
| A | ASP148 | |
| A | GLU279 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cev |
| Chain | Residue | Details |
| B | ASP148 | |
| B | GLU279 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cev |
| Chain | Residue | Details |
| C | ASP148 | |
| C | GLU279 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cev |
| Chain | Residue | Details |
| D | ASP148 | |
| D | GLU279 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cev |
| Chain | Residue | Details |
| E | ASP148 | |
| E | GLU279 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cev |
| Chain | Residue | Details |
| F | ASP148 | |
| F | GLU279 |
