6MM1
Structure of the cysteine-rich region from human EHMT2
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0002039 | molecular_function | p53 binding |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016279 | molecular_function | protein-lysine N-methyltransferase activity |
| A | 0042054 | molecular_function | histone methyltransferase activity |
| B | 0002039 | molecular_function | p53 binding |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0016279 | molecular_function | protein-lysine N-methyltransferase activity |
| B | 0042054 | molecular_function | histone methyltransferase activity |
| C | 0002039 | molecular_function | p53 binding |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0016279 | molecular_function | protein-lysine N-methyltransferase activity |
| C | 0042054 | molecular_function | histone methyltransferase activity |
| D | 0002039 | molecular_function | p53 binding |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0016279 | molecular_function | protein-lysine N-methyltransferase activity |
| D | 0042054 | molecular_function | histone methyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 601 |
| Chain | Residue |
| A | CYS426 |
| A | CYS428 |
| A | HIS491 |
| A | HIS535 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 602 |
| Chain | Residue |
| A | CYS494 |
| A | CYS497 |
| A | HIS520 |
| A | CYS523 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 603 |
| Chain | Residue |
| A | CYS459 |
| A | CYS481 |
| A | HIS484 |
| A | CYS446 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 604 |
| Chain | Residue |
| A | CYS509 |
| A | HIS517 |
| A | CYS533 |
| A | CYS536 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 601 |
| Chain | Residue |
| B | CYS426 |
| B | CYS428 |
| B | HIS491 |
| B | HIS535 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 602 |
| Chain | Residue |
| B | CYS494 |
| B | CYS497 |
| B | HIS520 |
| B | CYS523 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 603 |
| Chain | Residue |
| B | CYS446 |
| B | CYS459 |
| B | CYS481 |
| B | HIS484 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 604 |
| Chain | Residue |
| B | CYS509 |
| B | HIS517 |
| B | CYS533 |
| B | CYS536 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue ZN C 601 |
| Chain | Residue |
| C | CYS426 |
| C | CYS428 |
| C | HIS491 |
| C | HIS535 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN C 602 |
| Chain | Residue |
| C | CYS494 |
| C | CYS497 |
| C | HIS520 |
| C | CYS523 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN C 603 |
| Chain | Residue |
| C | CYS446 |
| C | CYS459 |
| C | CYS481 |
| C | HIS484 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue ZN C 604 |
| Chain | Residue |
| C | CYS509 |
| C | HIS517 |
| C | CYS533 |
| C | CYS536 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue ZN D 601 |
| Chain | Residue |
| D | CYS426 |
| D | CYS428 |
| D | HIS491 |
| D | HIS535 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue ZN D 602 |
| Chain | Residue |
| D | CYS494 |
| D | CYS497 |
| D | HIS520 |
| D | CYS523 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue ZN D 603 |
| Chain | Residue |
| D | CYS446 |
| D | CYS459 |
| D | CYS481 |
| D | HIS484 |
| site_id | AD7 |
| Number of Residues | 4 |
| Details | binding site for residue ZN D 604 |
| Chain | Residue |
| D | CYS509 |
| D | HIS517 |
| D | CYS533 |
| D | CYS536 |
