1MLV
Structure and Catalytic Mechanism of a SET Domain Protein Methyltransferase
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A, B, C (A, B, C) | Ribulose-1,5 biphosphate carboxylase/oxygenase large subunit N-methyltransferase | polymer | 444 | 50629.2 | 3 | UniProt (Q43088) Pfam (PF09273) | Pisum sativum (pea) | [Ribulose-biphosphate-carboxylase]-lysine N-methyltransferase, RuBisCO methyltransferase, Rubisco LSMT, rbcMT |
| 2 | D, F, H (A, B, C) | S-ADENOSYL-L-HOMOCYSTEINE | non-polymer | 384.4 | 3 | Chemie (SAH) | |||
| 3 | E, G, I (A, B, C) | 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID | non-polymer | 238.3 | 3 | Chemie (EPE) | |||
| 4 | J, K, L (A, B, C) | water | water | 18.0 | 666 | Chemie (HOH) |
Sequence modifications
A, B, C: 46 - 482 (UniProt: Q43088)
| PDB | External Database | Details |
|---|---|---|
| Met 45 | - | initiating methionine |
| Glu 483 | - | engineered mutation |
| Asn 484 | - | engineered mutation |
| Leu 485 | - | engineered mutation |
| Tyr 486 | - | engineered mutation |
| Phe 487 | - | engineered mutation |
| Gln 488 | - | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 3 |
| Total formula weight | 151887.5 | |
| Non-Polymers* | Number of molecules | 6 |
| Total formula weight | 1868.1 | |
| All* | Total formula weight | 153755.6 |
