5G3O
Bacillus cereus formamidase (BceAmiF) inhibited with urea.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004328 | molecular_function | formamidase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0033388 | biological_process | putrescine biosynthetic process from arginine |
| A | 0050126 | molecular_function | N-carbamoylputrescine amidase activity |
| B | 0004328 | molecular_function | formamidase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0033388 | biological_process | putrescine biosynthetic process from arginine |
| B | 0050126 | molecular_function | N-carbamoylputrescine amidase activity |
| C | 0004328 | molecular_function | formamidase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0033388 | biological_process | putrescine biosynthetic process from arginine |
| C | 0050126 | molecular_function | N-carbamoylputrescine amidase activity |
| D | 0004328 | molecular_function | formamidase activity |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0033388 | biological_process | putrescine biosynthetic process from arginine |
| D | 0050126 | molecular_function | N-carbamoylputrescine amidase activity |
| E | 0004328 | molecular_function | formamidase activity |
| E | 0016787 | molecular_function | hydrolase activity |
| E | 0033388 | biological_process | putrescine biosynthetic process from arginine |
| E | 0050126 | molecular_function | N-carbamoylputrescine amidase activity |
| F | 0004328 | molecular_function | formamidase activity |
| F | 0016787 | molecular_function | hydrolase activity |
| F | 0033388 | biological_process | putrescine biosynthetic process from arginine |
| F | 0050126 | molecular_function | N-carbamoylputrescine amidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PEG B 1308 |
| Chain | Residue |
| B | GLU197 |
| B | HOH2074 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG A 1309 |
| Chain | Residue |
| A | GLU197 |
| A | HOH2093 |
| C | THR241 |
| F | ARG204 |
| F | THR240 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PEG B 1309 |
| Chain | Residue |
| B | ASN293 |
| B | PRO294 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG E 1308 |
| Chain | Residue |
| B | THR241 |
| D | HOH2048 |
| E | GLU197 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE PEG F 1308 |
| Chain | Residue |
| F | GLU197 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG C 1308 |
| Chain | Residue |
| C | VAL151 |
| C | LYS159 |
| C | LYS180 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PEG E 1309 |
| Chain | Residue |
| E | MET126 |
| E | ILE127 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG D 1308 |
| Chain | Residue |
| D | ASN293 |
| D | PRO294 |
| D | LYS299 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG E 1310 |
| Chain | Residue |
| E | GLN38 |
| E | TRP250 |
| F | ASP223 |
| F | GLY224 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG D 1309 |
| Chain | Residue |
| D | VAL151 |
| D | ASP153 |
| D | LYS159 |
| D | LYS180 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PEG C 1309 |
| Chain | Residue |
| C | ASN293 |
| C | HOH2069 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PEG F 1309 |
| Chain | Residue |
| F | ASP153 |
| F | LYS159 |
| site_id | BC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PEG D 1310 |
| Chain | Residue |
| A | THR241 |
| D | GLU197 |
| site_id | BC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PEG B 1310 |
| Chain | Residue |
| B | ASP153 |
| B | LYS159 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG E 1311 |
| Chain | Residue |
| E | VAL151 |
| E | ASP153 |
| E | LYS159 |
| E | HOH2041 |
| site_id | BC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PEG D 1311 |
| Chain | Residue |
| D | LYS41 |
| D | TRP250 |
| site_id | BC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PEG A 1310 |
| Chain | Residue |
| A | ASN293 |
| A | PRO294 |
| site_id | BC9 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE PEG F 1310 |
| Chain | Residue |
| F | SER48 |
| site_id | CC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG A 1311 |
| Chain | Residue |
| A | VAL151 |
| A | ASP153 |
| A | LYS159 |
| site_id | CC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG E 1312 |
| Chain | Residue |
| E | ASN293 |
| E | PRO294 |
| E | LYS299 |
| site_id | CC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG F 1311 |
| Chain | Residue |
| A | GLY148 |
| F | ASN293 |
| F | PRO294 |
| site_id | CC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PEG C 1310 |
| Chain | Residue |
| C | GLU197 |
| D | THR241 |
| site_id | CC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE PEG B 1311 |
| Chain | Residue |
| B | MET126 |
| site_id | CC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PG4 A 1312 |
| Chain | Residue |
| A | LYS41 |
| A | TRP250 |
| D | ASP223 |
| D | GLY224 |
| site_id | CC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PG4 A 1313 |
| Chain | Residue |
| A | ASP223 |
| A | GLY224 |
| C | GLN38 |
| C | LYS41 |
| site_id | CC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE P4G C 1311 |
| Chain | Residue |
| C | ASN236 |
| C | PHE237 |
| C | HOH2070 |
| F | PHE237 |
| F | ALA255 |
| F | GLU256 |
| F | TYR258 |
| site_id | CC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE P4G F 1312 |
| Chain | Residue |
| B | ASP223 |
| F | LYS41 |
| site_id | DC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 C 1312 |
| Chain | Residue |
| A | HIS246 |
| A | ARG247 |
| A | ASN248 |
| C | HIS246 |
| C | ARG247 |
| C | ASN248 |
| D | HIS246 |
| D | ARG247 |
| D | ASN248 |
| site_id | DC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 B 1312 |
| Chain | Residue |
| B | HIS246 |
| B | ARG247 |
| B | ASN248 |
| E | HIS246 |
| E | ARG247 |
| E | ASN248 |
| F | HIS246 |
| F | ARG247 |
| F | ASN248 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01243","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_01243","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_01243","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |






