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... (A, B, C, D, E...) | Leucine carboxyl methyltransferase 1 | polymer | 334 | 38504.2 | 8 | UniProt (Q9UIC8) Pfam (PF04072) | Homo sapiens (human) | Protein-leucine O-methyltransferase |
| 2 | I, K, N, P, S... (A, B, C, D, E...) | S-ADENOSYL-L-HOMOCYSTEINE | non-polymer | 384.4 | 8 | Chemie (SAH) | |||
| 3 | BA, J, M, O, R... (H, A, B, C, D...) | GLYCEROL | non-polymer | 92.1 | 8 | Chemie (GOL) | |||
| 4 | AA, L, Q, T (H, B, D, E) | 2-(N-MORPHOLINO)-ETHANESULFONIC ACID | non-polymer | 195.2 | 4 | Chemie (MES) | |||
| 5 | CA, DA, EA, FA, GA... (A, B, C, D, E...) | 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 |
