4R85
Crystal structure of 5-methylcytosine deaminase from Klebsiella pneumoniae liganded with 5-methylcytosine
Replaces: 4JNPFunctional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| B | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| C | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| D | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| E | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| F | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE 17E A 501 |
| Chain | Residue |
| A | HIS58 |
| A | ASP308 |
| A | SER309 |
| A | TRP314 |
| A | FE2502 |
| A | HOH601 |
| A | LEU76 |
| A | PHE149 |
| A | GLN151 |
| A | ILE178 |
| A | HIS209 |
| A | GLU212 |
| A | HIS241 |
| A | GLU273 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE2 A 502 |
| Chain | Residue |
| A | HIS56 |
| A | HIS58 |
| A | HIS209 |
| A | HIS241 |
| A | ASP308 |
| A | 17E501 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A 503 |
| Chain | Residue |
| A | ARG185 |
| A | GLN217 |
| A | ARG219 |
| A | PHE220 |
| A | GLU222 |
| A | VAL223 |
| A | HOH647 |
| A | HOH669 |
| A | HOH715 |
| A | HOH746 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 504 |
| Chain | Residue |
| A | PRO123 |
| A | LEU125 |
| A | ARG166 |
| A | HOH833 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 505 |
| Chain | Residue |
| A | ASP327 |
| A | ALA328 |
| A | HOH828 |
| A | HOH894 |
| D | ASP327 |
| D | ALA328 |
| D | HIS331 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE 17E B 501 |
| Chain | Residue |
| B | HIS58 |
| B | LEU76 |
| B | PHE149 |
| B | GLN151 |
| B | ILE178 |
| B | HIS209 |
| B | GLU212 |
| B | HIS241 |
| B | GLU273 |
| B | ASP308 |
| B | SER309 |
| B | TRP314 |
| B | FE2502 |
| B | HOH610 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE2 B 502 |
| Chain | Residue |
| B | HIS56 |
| B | HIS58 |
| B | HIS209 |
| B | HIS241 |
| B | ASP308 |
| B | 17E501 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 503 |
| Chain | Residue |
| B | PRO92 |
| B | GLU93 |
| B | ALA130 |
| B | HOH670 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 504 |
| Chain | Residue |
| B | SER254 |
| B | PHE257 |
| B | ARG292 |
| B | GLU295 |
| B | HOH611 |
| B | HOH662 |
| B | HOH747 |
| B | HOH785 |
| site_id | BC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL B 505 |
| Chain | Residue |
| B | ARG185 |
| B | GLN217 |
| B | ARG219 |
| B | PHE220 |
| B | GLU222 |
| B | VAL223 |
| B | HOH635 |
| B | HOH700 |
| B | HOH738 |
| B | HOH743 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 506 |
| Chain | Residue |
| B | GLN145 |
| B | ASP173 |
| B | LEU356 |
| B | CYS357 |
| site_id | BC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE 17E C 501 |
| Chain | Residue |
| C | FE2502 |
| C | HOH621 |
| C | HIS58 |
| C | LEU76 |
| C | PHE149 |
| C | GLN151 |
| C | ILE178 |
| C | HIS209 |
| C | GLU212 |
| C | HIS241 |
| C | GLU273 |
| C | ASP308 |
| C | SER309 |
| C | TRP314 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE2 C 502 |
| Chain | Residue |
| C | HIS56 |
| C | HIS58 |
| C | HIS209 |
| C | HIS241 |
| C | ASP308 |
| C | 17E501 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL C 503 |
| Chain | Residue |
| C | ASP327 |
| C | ALA328 |
| E | ASP327 |
| E | ALA328 |
| E | HIS331 |
| E | HOH882 |
| site_id | BC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL C 504 |
| Chain | Residue |
| C | ARG185 |
| C | GLN217 |
| C | ARG219 |
| C | PHE220 |
| C | GLU222 |
| C | VAL223 |
| C | HOH645 |
| C | HOH801 |
| site_id | BC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL C 505 |
| Chain | Residue |
| C | SER254 |
| C | PHE257 |
| C | ARG292 |
| C | GLU295 |
| C | HOH618 |
| C | HOH647 |
| E | HOH706 |
| site_id | BC8 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE 17E D 501 |
| Chain | Residue |
| D | HIS58 |
| D | LEU76 |
| D | PHE149 |
| D | GLN151 |
| D | ILE178 |
| D | GLU212 |
| D | HIS241 |
| D | GLU273 |
| D | ASP308 |
| D | SER309 |
| D | TRP314 |
| D | FE2502 |
| D | HOH604 |
| site_id | BC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE2 D 502 |
| Chain | Residue |
| D | HIS56 |
| D | HIS58 |
| D | HIS209 |
| D | HIS241 |
| D | ASP308 |
| D | 17E501 |
| site_id | CC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL D 503 |
| Chain | Residue |
| D | SER254 |
| D | PHE257 |
| D | ARG292 |
| D | GLU295 |
| D | HOH618 |
| D | HOH625 |
| D | HOH783 |
| site_id | CC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL D 504 |
| Chain | Residue |
| D | ARG185 |
| D | GLN217 |
| D | ARG219 |
| D | PHE220 |
| D | GLU222 |
| D | VAL223 |
| D | HOH645 |
| D | HOH666 |
| D | HOH707 |
| D | HOH740 |
| site_id | CC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE 17E E 501 |
| Chain | Residue |
| E | HIS58 |
| E | LEU76 |
| E | PHE149 |
| E | GLN151 |
| E | ILE178 |
| E | GLU212 |
| E | HIS241 |
| E | GLU273 |
| E | ASP308 |
| E | SER309 |
| E | TRP314 |
| E | FE2502 |
| E | HOH617 |
| site_id | CC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE2 E 502 |
| Chain | Residue |
| E | HIS56 |
| E | HIS58 |
| E | HIS209 |
| E | HIS241 |
| E | ASP308 |
| E | 17E501 |
| site_id | CC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL E 503 |
| Chain | Residue |
| E | ARG185 |
| E | GLN217 |
| E | ARG219 |
| E | PHE220 |
| E | GLU222 |
| E | VAL223 |
| E | HOH618 |
| E | HOH751 |
| E | HOH764 |
| site_id | CC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL E 504 |
| Chain | Residue |
| E | SER254 |
| E | PHE257 |
| E | ARG292 |
| E | GLU295 |
| E | HOH619 |
| E | HOH776 |
| E | HOH802 |
| site_id | CC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL E 505 |
| Chain | Residue |
| E | HIS113 |
| E | ASP143 |
| E | ASN361 |
| E | PRO369 |
| E | ASN371 |
| E | ARG395 |
| E | HIS396 |
| E | HOH841 |
| site_id | CC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL F 501 |
| Chain | Residue |
| B | ASP327 |
| B | ALA328 |
| B | HIS331 |
| F | ASP327 |
| F | ALA328 |
| F | HOH878 |
| site_id | CC9 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE 17E F 502 |
| Chain | Residue |
| F | HIS58 |
| F | LEU76 |
| F | PHE149 |
| F | GLN151 |
| F | ILE178 |
| F | HIS209 |
| F | GLU212 |
| F | HIS241 |
| F | GLU273 |
| F | ASP308 |
| F | SER309 |
| F | TRP314 |
| F | FE2503 |
| F | HOH620 |
| site_id | DC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE2 F 503 |
| Chain | Residue |
| F | HIS56 |
| F | HIS58 |
| F | HIS209 |
| F | HIS241 |
| F | ASP308 |
| F | 17E502 |
| site_id | DC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL F 504 |
| Chain | Residue |
| F | ARG185 |
| F | GLN217 |
| F | ARG219 |
| F | PHE220 |
| F | GLU222 |
| F | VAL223 |
| F | HOH650 |
| F | HOH793 |
| site_id | DC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL F 505 |
| Chain | Residue |
| B | HOH705 |
| F | SER254 |
| F | PHE257 |
| F | ARG292 |
| F | GLU295 |
| F | HOH631 |
