Research workbench
2-enoyl-CoA hydratase, data collected at 100 K, pH 6.5
Analyse 2-enoyl-CoA hydratase, data collected at 100 K, pH 6.5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1DUB
- Type
- protein
- Length
- 1,557 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P14604
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D, E | — | protein | 260 | — | P14604 |
| B, C, F | — | protein | 259 | — | P14604 |
Compared structures
- 1DUB · 2-enoyl-CoA hydratase, data collected at 100 K, pH 6.5 · the same entry in another collection · chain F against F, TM-score 1.00
- P14604 · AlphaFold monomer V2.0 prediction for enoyl-CoA hydratase, mitochondrial (P14604) · a predicted model of the same protein · chain E 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 P14604
- Elsewhere: RCSB PDB 1DUB · PDBe 1DUB · UniProt P14604
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