3KHC
Crystal Structure of Escherichia coli AlkB in complex with ssDNA containing a 1-methylguanine lesion
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006281 | biological_process | DNA repair |
| A | 0006307 | biological_process | DNA alkylation repair |
| A | 0008198 | molecular_function | ferrous iron binding |
| A | 0035513 | biological_process | oxidative RNA demethylation |
| A | 0035515 | molecular_function | oxidative RNA demethylase activity |
| A | 0035516 | molecular_function | broad specificity oxidative DNA demethylase activity |
| A | 0042245 | biological_process | RNA repair |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051213 | molecular_function | dioxygenase activity |
| A | 0070989 | biological_process | oxidative demethylation |
| A | 0072702 | biological_process | response to methyl methanesulfonate |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006281 | biological_process | DNA repair |
| B | 0006307 | biological_process | DNA alkylation repair |
| B | 0008198 | molecular_function | ferrous iron binding |
| B | 0035513 | biological_process | oxidative RNA demethylation |
| B | 0035515 | molecular_function | oxidative RNA demethylase activity |
| B | 0035516 | molecular_function | broad specificity oxidative DNA demethylase activity |
| B | 0042245 | biological_process | RNA repair |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051213 | molecular_function | dioxygenase activity |
| B | 0070989 | biological_process | oxidative demethylation |
| B | 0072702 | biological_process | response to methyl methanesulfonate |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CO A 217 |
| Chain | Residue |
| A | HIS131 |
| A | ASP133 |
| A | HIS187 |
| A | HOH245 |
| A | AKG400 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE AKG A 400 |
| Chain | Residue |
| A | HIS131 |
| A | ASP133 |
| A | SER145 |
| A | HIS187 |
| A | ILE189 |
| A | ARG204 |
| A | ASN206 |
| A | THR208 |
| A | CO217 |
| A | HOH220 |
| A | HOH230 |
| A | HOH245 |
| A | LEU118 |
| A | ASN120 |
| A | TYR122 |
| A | LEU128 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CO B 217 |
| Chain | Residue |
| B | HIS131 |
| B | ASP133 |
| B | HIS187 |
| B | HOH260 |
| B | AKG401 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE AKG B 401 |
| Chain | Residue |
| B | LEU118 |
| B | ASN120 |
| B | TYR122 |
| B | LEU128 |
| B | HIS131 |
| B | ASP133 |
| B | HIS187 |
| B | ILE189 |
| B | ARG204 |
| B | ASN206 |
| B | THR208 |
| B | ARG210 |
| B | CO217 |
| B | HOH260 |
| B | HOH298 |
| C | MG14 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16482161, ECO:0000269|PubMed:20084272 |
| Chain | Residue | Details |
| A | TRP69 | |
| A | ALA135 | |
| A | ARG161 | |
| B | TRP69 | |
| B | ALA135 | |
| B | ARG161 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | TYR76 | |
| A | ASN120 | |
| A | ARG204 | |
| B | TYR76 | |
| B | ASN120 | |
| B | ARG204 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00805, ECO:0000269|PubMed:16482161 |
| Chain | Residue | Details |
| A | HIS131 | |
| A | ASP133 | |
| A | HIS187 | |
| B | HIS131 | |
| B | ASP133 | |
| B | HIS187 |
