3IEI
Crystal structure of human leucine carboxylmethyltransferase-1 in complex with S-adenosyl homocysteine
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, D, E... | Leucine carboxyl methyltransferase 1 | polymer | 334 | 38504.2 | 8 | UniProt (Q9UIC8) Pfam (PF04072) In PDB | Homo sapiens (human) | Protein-leucine O-methyltransferase |
2 | A, B, C, D, E... | S-ADENOSYL-L-HOMOCYSTEINE | non-polymer | 384.4 | 8 | Chemie (SAH) | |||
3 | H, A, B, C, D... | GLYCEROL | non-polymer | 92.1 | 8 | Chemie (GOL) | |||
4 | H, B, D, E | 2-(N-MORPHOLINO)-ETHANESULFONIC ACID | non-polymer | 195.2 | 4 | Chemie (MES) | |||
5 | water | water | 18.0 | 1851 | Chemie (HOH) |
Sequence modifications
A, B, C, D, E, F, G, H: 1 - 334 (UniProt: Q9UIC8)
PDB | External Database | Details |
---|---|---|
Met 19 | Cys 19 | engineered mutation |
Glu 21 | Ala 21 | engineered mutation |
Asn 22 | Asp 22 | engineered mutation |
Ser 115 | Pro 115 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 8 |
Total formula weight | 308033.7 | |
Non-Polymers* | Number of molecules | 20 |
Total formula weight | 4593.0 | |
All* | Total formula weight | 312626.7 |