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Crystal structure of human L-3- hydroxyacyl-CoA dehydrogenase (EC1.1.1.35) from mitochondria at the resolution 2.0 a, northeast structural genomics consortium target HR487, mitochondrial protein partnership
Analyse Crystal structure of human L-3- hydroxyacyl-CoA dehydrogenase (EC1.1.1.35) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3RQS
- Type
- protein
- Length
- 608 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q16836
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 292 | — | Q16836 |
| B | — | protein | 316 | — | Q16836 |
Compared structures
- 3RQS · Crystal Structure of human L-3- Hydroxyacyl-CoA dehydrogenase (EC1.1.1.35) from… · the same entry in another collection · chain A against A, TM-score 1.00
- Q16836 · AlphaFold monomer V2.0 prediction for hydroxyacyl-coenzyme a dehydrogenase, mitochondrial… · 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 Q16836
- Elsewhere: RCSB PDB 3RQS · PDBe 3RQS · UniProt Q16836
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