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 | Ribulose-1,5 biphosphate carboxylase/oxygenase large subunit N-methyltransferase | polymer | 444 | 50629.2 | 3 | UniProt (Q43088) Pfam (PF09273) In PDB | Pisum sativum (pea) | [Ribulose-biphosphate-carboxylase]-lysine N-methyltransferase, RuBisCO methyltransferase, Rubisco LSMT, rbcMT |
2 | A, B, C | S-ADENOSYL-L-HOMOCYSTEINE | non-polymer | 384.4 | 3 | Chemie (SAH) | |||
3 | A, B, C | 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID | non-polymer | 238.3 | 3 | Chemie (EPE) | |||
4 | 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 |