Research workbench
Crystal structure of human leucine carboxylmethyltransferase-1 in complex with S-adenosyl homocysteine
Analyse Crystal structure of human leucine carboxylmethyltransferase-1 in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3IEI
- Type
- protein
- Length
- 2,488 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9UIC8
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H | — | protein | 311 | — | Q9UIC8 |
Compared structures
- 3IEI · Crystal structure of human leucine carboxylmethyltransferase-1 in complex with S-adenosyl… · the same entry in another collection · chain G against G, TM-score 1.00
- Q9UIC8 · AlphaFold monomer V2.0 prediction for leucine carboxyl methyltransferase 1 (Q9UIC8) · a predicted model of the same protein · chain A against A, TM-score 0.99
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q9UIC8
- Elsewhere: RCSB PDB 3IEI · PDBe 3IEI · UniProt Q9UIC8
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