4R7W
Crystal structure of 5-methylcytosine deaminase from Klebsiella pneumoniae liganded with phosphonocytosine
Replaces: 4JNSFunctional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004131 | molecular_function | cytosine deaminase activity |
A | 0006209 | biological_process | cytosine catabolic process |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
A | 0035888 | molecular_function | isoguanine deaminase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0004131 | molecular_function | cytosine deaminase activity |
B | 0006209 | biological_process | cytosine catabolic process |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
B | 0035888 | molecular_function | isoguanine deaminase activity |
B | 0046872 | molecular_function | metal ion binding |
C | 0004131 | molecular_function | cytosine deaminase activity |
C | 0006209 | biological_process | cytosine catabolic process |
C | 0016787 | molecular_function | hydrolase activity |
C | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
C | 0035888 | molecular_function | isoguanine deaminase activity |
C | 0046872 | molecular_function | metal ion binding |
D | 0004131 | molecular_function | cytosine deaminase activity |
D | 0006209 | biological_process | cytosine catabolic process |
D | 0016787 | molecular_function | hydrolase activity |
D | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
D | 0035888 | molecular_function | isoguanine deaminase activity |
D | 0046872 | molecular_function | metal ion binding |
E | 0004131 | molecular_function | cytosine deaminase activity |
E | 0006209 | biological_process | cytosine catabolic process |
E | 0016787 | molecular_function | hydrolase activity |
E | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
E | 0035888 | molecular_function | isoguanine deaminase activity |
E | 0046872 | molecular_function | metal ion binding |
F | 0004131 | molecular_function | cytosine deaminase activity |
F | 0006209 | biological_process | cytosine catabolic process |
F | 0016787 | molecular_function | hydrolase activity |
F | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
F | 0035888 | molecular_function | isoguanine deaminase activity |
F | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FE2 A 501 |
Chain | Residue |
A | HIS56 |
A | HIS58 |
A | HIS209 |
A | HIS241 |
A | ASP308 |
A | O7U502 |
site_id | AC2 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE O7U A 502 |
Chain | Residue |
A | GLN151 |
A | HIS209 |
A | GLU212 |
A | HIS241 |
A | GLU273 |
A | LEU277 |
A | ASP308 |
A | TRP314 |
A | FE2501 |
A | HOH605 |
A | HIS58 |
A | LEU76 |
A | PHE149 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PEG A 503 |
Chain | Residue |
A | ASP327 |
A | ALA328 |
A | HIS331 |
B | ASP327 |
B | ALA328 |
B | HIS331 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 504 |
Chain | Residue |
A | ASP214 |
A | PRO216 |
A | ARG287 |
A | HOH679 |
B | PRO285 |
D | ASP249 |
D | HOH657 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 505 |
Chain | Residue |
A | ASP376 |
A | ARG386 |
A | GLN387 |
A | ALA388 |
A | ARG389 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FE2 B 501 |
Chain | Residue |
B | HIS56 |
B | HIS58 |
B | HIS209 |
B | HIS241 |
B | ASP308 |
B | O7U502 |
site_id | AC7 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE O7U B 502 |
Chain | Residue |
B | HIS58 |
B | LEU76 |
B | PHE149 |
B | GLN151 |
B | ILE178 |
B | HIS209 |
B | GLU212 |
B | HIS241 |
B | GLU273 |
B | LEU277 |
B | ASP308 |
B | TRP314 |
B | FE2501 |
B | HOH609 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO B 503 |
Chain | Residue |
B | SER254 |
B | PHE257 |
B | ARG258 |
B | HOH783 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FE2 C 501 |
Chain | Residue |
C | HIS56 |
C | HIS58 |
C | HIS209 |
C | HIS241 |
C | ASP308 |
C | O7U502 |
site_id | BC1 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE O7U C 502 |
Chain | Residue |
C | HIS58 |
C | LEU76 |
C | PHE149 |
C | GLN151 |
C | HIS209 |
C | GLU212 |
C | HIS241 |
C | GLU273 |
C | LEU277 |
C | ASP308 |
C | TRP314 |
C | FE2501 |
C | HOH601 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL C 503 |
Chain | Residue |
C | SER254 |
C | PHE257 |
C | ARG292 |
C | GLU295 |
C | HOH668 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PEG C 504 |
Chain | Residue |
C | ALA328 |
E | ASP327 |
E | ALA328 |
site_id | BC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE PEG C 505 |
Chain | Residue |
A | LYS255 |
C | PRO179 |
C | HIS180 |
C | GLU182 |
C | THR184 |
C | ARG185 |
C | GLN217 |
C | PHE220 |
C | HOH692 |
C | HOH743 |
site_id | BC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO C 506 |
Chain | Residue |
C | GLU404 |
C | VAL405 |
C | GLU406 |
C | HOH681 |
E | VAL405 |
C | ARG389 |
site_id | BC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FE2 D 501 |
Chain | Residue |
D | HIS56 |
D | HIS58 |
D | HIS209 |
D | HIS241 |
D | ASP308 |
D | O7U502 |
site_id | BC7 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE O7U D 502 |
Chain | Residue |
D | HIS58 |
D | LEU76 |
D | GLN151 |
D | HIS209 |
D | GLU212 |
D | HIS241 |
D | GLU273 |
D | LEU277 |
D | ASP308 |
D | TRP314 |
D | FE2501 |
site_id | BC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PEG D 503 |
Chain | Residue |
D | ASP327 |
D | ALA328 |
D | HIS331 |
F | ASP327 |
F | ALA328 |
F | HIS331 |
site_id | BC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO D 504 |
Chain | Residue |
D | ARG72 |
D | ARG280 |
F | ARG298 |
F | HIS334 |
site_id | CC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FE2 E 501 |
Chain | Residue |
E | HIS56 |
E | HIS58 |
E | HIS209 |
E | HIS241 |
E | ASP308 |
E | O7U502 |
site_id | CC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE O7U E 502 |
Chain | Residue |
E | HIS58 |
E | LEU76 |
E | PHE149 |
E | GLN151 |
E | ILE178 |
E | HIS209 |
E | GLU212 |
E | HIS241 |
E | GLU273 |
E | LEU277 |
E | ASP308 |
E | TRP314 |
E | FE2501 |
E | HOH607 |
site_id | CC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO E 503 |
Chain | Residue |
E | ASN319 |
E | ASN321 |
E | ARG324 |
E | GLN387 |
site_id | CC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PEG E 504 |
Chain | Residue |
E | ALA65 |
E | HOH830 |
E | HOH840 |
site_id | CC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FE2 F 501 |
Chain | Residue |
F | HIS56 |
F | HIS58 |
F | HIS209 |
F | HIS241 |
F | ASP308 |
F | O7U502 |
site_id | CC6 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE O7U F 502 |
Chain | Residue |
F | HIS58 |
F | LEU76 |
F | GLN151 |
F | ILE178 |
F | HIS209 |
F | GLU212 |
F | HIS241 |
F | GLU273 |
F | LEU277 |
F | ASP308 |
F | TRP314 |
F | FE2501 |