MolNFT v1 · #50938 · protein
Correlation of X-ray deduced and experimental amino acid sequences of trimethylamine dehydrogenase
2TMD: “Correlation of X-ray deduced and experimental amino acid sequences of trimethylamine dehydrogenase”. X-ray diffraction. MolNFT v1 #50938 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2TMD
- Type
- protein
- Length
- 1,458 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P16099
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 729 | — | P16099 |
Compared structures
- 2TMD · Correlation of X-ray deduced and experimental amino acid sequences of trimethylamine… · the same entry in another collection · chain A against A, TM-score 1.00
- P16099 · AlphaFold monomer V2.0 prediction for trimethylamine dehydrogenase (P16099) · a predicted model of the same protein · chain A against A, TM-score 1.00
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 P16099
- Elsewhere: RCSB PDB 2TMD · PDBe 2TMD · UniProt P16099
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