4KEA
Crystal structure of D196N mutant of Monoglyceride lipase from Bacillus sp. H257 in space group P212121
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0047372 | molecular_function | monoacylglycerol lipase activity |
| A | 0052689 | molecular_function | carboxylic ester hydrolase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0047372 | molecular_function | monoacylglycerol lipase activity |
| B | 0052689 | molecular_function | carboxylic ester hydrolase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0047372 | molecular_function | monoacylglycerol lipase activity |
| C | 0052689 | molecular_function | carboxylic ester hydrolase activity |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0047372 | molecular_function | monoacylglycerol lipase activity |
| D | 0052689 | molecular_function | carboxylic ester hydrolase activity |
| E | 0016787 | molecular_function | hydrolase activity |
| E | 0047372 | molecular_function | monoacylglycerol lipase activity |
| E | 0052689 | molecular_function | carboxylic ester hydrolase activity |
| F | 0016787 | molecular_function | hydrolase activity |
| F | 0047372 | molecular_function | monoacylglycerol lipase activity |
| F | 0052689 | molecular_function | carboxylic ester hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MPD A 301 |
| Chain | Residue |
| A | PHE29 |
| A | THR30 |
| A | LEU96 |
| A | GLU156 |
| A | ALA158 |
| A | VAL227 |
| A | HOH419 |
| A | HOH431 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD A 302 |
| Chain | Residue |
| A | VAL198 |
| A | HOH570 |
| B | MPD303 |
| A | SER97 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD A 303 |
| Chain | Residue |
| A | GLU239 |
| A | ARG240 |
| A | GLU243 |
| C | LYS247 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD A 304 |
| Chain | Residue |
| A | ASP231 |
| A | TYR232 |
| A | PRO235 |
| A | HOH462 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD A 305 |
| Chain | Residue |
| A | VAL21 |
| A | GLY47 |
| A | TYR48 |
| A | ALA249 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MPD A 306 |
| Chain | Residue |
| A | LEU8 |
| A | LEU157 |
| A | ALA158 |
| A | TYR159 |
| A | GLU160 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MPD B 301 |
| Chain | Residue |
| B | GLY28 |
| B | PHE29 |
| B | THR30 |
| B | LEU96 |
| B | GLU156 |
| B | VAL227 |
| B | MPD302 |
| B | HOH401 |
| B | HOH411 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD B 302 |
| Chain | Residue |
| B | PHE29 |
| B | SER97 |
| B | MPD301 |
| B | HOH402 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MPD B 303 |
| Chain | Residue |
| A | ALA127 |
| A | MPD302 |
| B | ASP143 |
| B | MPD304 |
| B | HOH437 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD B 304 |
| Chain | Residue |
| B | ASP143 |
| B | ILE145 |
| B | MPD303 |
| B | HOH583 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD C 301 |
| Chain | Residue |
| C | PHE29 |
| C | SER97 |
| C | MPD302 |
| C | HOH401 |
| site_id | BC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MPD C 302 |
| Chain | Residue |
| C | THR30 |
| C | LEU96 |
| C | SER97 |
| C | GLU156 |
| C | ALA158 |
| C | MPD301 |
| C | HOH401 |
| C | HOH482 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD C 303 |
| Chain | Residue |
| C | GLN86 |
| C | ASP231 |
| C | GLN234 |
| C | PRO235 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MPD C 304 |
| Chain | Residue |
| C | GLY47 |
| C | TYR48 |
| C | HOH519 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MPD D 301 |
| Chain | Residue |
| D | PHE29 |
| D | GLY31 |
| D | GLU156 |
| D | HIS226 |
| D | MPD302 |
| D | HOH493 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MPD D 302 |
| Chain | Residue |
| D | SER97 |
| D | ILE125 |
| D | LEU170 |
| D | VAL198 |
| D | MPD301 |
| D | HOH517 |
| site_id | BC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MPD D 303 |
| Chain | Residue |
| D | ASN151 |
| D | ASP231 |
| D | TYR232 |
| site_id | BC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MPD E 301 |
| Chain | Residue |
| E | PHE29 |
| E | SER97 |
| E | ILE125 |
| E | LEU167 |
| E | LEU170 |
| E | VAL198 |
| E | MPD302 |
| E | HOH402 |
| site_id | CC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MPD E 302 |
| Chain | Residue |
| E | HOH552 |
| E | PHE29 |
| E | THR30 |
| E | LEU96 |
| E | GLU156 |
| E | VAL227 |
| E | MPD301 |
| site_id | CC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE MPD E 303 |
| Chain | Residue |
| E | VAL21 |
| E | ALA46 |
| E | GLY47 |
| E | TYR48 |
| E | ALA249 |
| E | HOH407 |
| F | ALA46 |
| F | TYR48 |
| F | HOH402 |
| F | HOH421 |
| site_id | CC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD E 304 |
| Chain | Residue |
| E | ASN151 |
| E | ASP231 |
| E | TYR232 |
| E | GLN234 |
| site_id | CC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD F 301 |
| Chain | Residue |
| F | PHE29 |
| F | SER97 |
| F | VAL198 |
| F | HOH462 |
| site_id | CC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MPD F 302 |
| Chain | Residue |
| F | PHE29 |
| F | GLU156 |
| F | ALA158 |
| F | VAL227 |
| F | HOH463 |
| F | HOH504 |
| site_id | CC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MPD F 303 |
| Chain | Residue |
| F | ASN151 |
| F | LEU230 |
| F | ASP231 |
| F | TYR232 |
| F | GLN234 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Active site: {"description":"Nucleophile"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Active site: {"description":"Charge relay system"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Site: {"description":"Important for substrate specificity"} |
| Chain | Residue | Details |
