Research workbench
3-D structure of PHTET1-12S, dodecamer in the asymmetric unit
Analyse 3-D structure of PHTET1-12S, dodecamer in the asymmetric unit in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WYR
- Type
- protein
- Length
- 3,904 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O58255
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, H, J | — | protein | 326 | — | O58255 |
| B, D, G, I, K, L | — | protein | 325 | — | O58255 |
| F | — | protein | 324 | — | O58255 |
Compared structures
- 2WYR · 3-D structure of PhTET1-12s, dodecamer in the asymmetric unit · the same entry in another collection · 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 O58255
- Elsewhere: RCSB PDB 2WYR · PDBe 2WYR · UniProt O58255
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