2AR0
Crystal structure of Type I restriction enzyme EcoKI M protein (EC 2.1.1.72) (M.EcoKI)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003676 | molecular_function | nucleic acid binding |
A | 0003677 | molecular_function | DNA binding |
A | 0005515 | molecular_function | protein binding |
A | 0005829 | cellular_component | cytosol |
A | 0008168 | molecular_function | methyltransferase activity |
A | 0008170 | molecular_function | N-methyltransferase activity |
A | 0009007 | molecular_function | site-specific DNA-methyltransferase (adenine-specific) activity |
A | 0009307 | biological_process | DNA restriction-modification system |
A | 0016740 | molecular_function | transferase activity |
A | 0019812 | cellular_component | type I site-specific deoxyribonuclease complex |
A | 0032259 | biological_process | methylation |
B | 0003676 | molecular_function | nucleic acid binding |
B | 0003677 | molecular_function | DNA binding |
B | 0005515 | molecular_function | protein binding |
B | 0005829 | cellular_component | cytosol |
B | 0008168 | molecular_function | methyltransferase activity |
B | 0008170 | molecular_function | N-methyltransferase activity |
B | 0009007 | molecular_function | site-specific DNA-methyltransferase (adenine-specific) activity |
B | 0009307 | biological_process | DNA restriction-modification system |
B | 0016740 | molecular_function | transferase activity |
B | 0019812 | cellular_component | type I site-specific deoxyribonuclease complex |
B | 0032259 | biological_process | methylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE UNX A 1001 |
Chain | Residue |
A | UNX1002 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE UNX A 1002 |
Chain | Residue |
A | ARG519 |
A | UNX1001 |
A | UNX1004 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE UNX A 1003 |
Chain | Residue |
A | TRP13 |
B | ARG519 |
site_id | AC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE UNX A 1004 |
Chain | Residue |
A | TYR26 |
A | UNX1002 |
site_id | AC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE UNX A 1006 |
Chain | Residue |
A | UNX1008 |
site_id | AC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE UNX A 1007 |
Chain | Residue |
A | ARG519 |
A | UNX1009 |
site_id | AC7 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE UNX A 1008 |
Chain | Residue |
A | UNX1006 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE UNX A 1009 |
Chain | Residue |
A | ARG519 |
A | UNX1007 |
B | ARG519 |
Functional Information from PROSITE/UniProt
site_id | PS00092 |
Number of Residues | 7 |
Details | N6_MTASE N-6 Adenine-specific DNA methylases signature. VATNPPF |
Chain | Residue | Details |
A | VAL265-PHE271 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q89Z59 |
Chain | Residue | Details |
A | GLN150 | |
A | THR180 | |
A | GLU218 | |
B | GLN150 | |
B | THR180 | |
B | GLU218 |