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Crystal structure of hydroxymethylglutaryl-CoA reductase from elizabethkingia anophelis NUHP1
Analyse Crystal structure of hydroxymethylglutaryl-CoA reductase from elizabethkingia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7N7S
- Type
- protein
- Length
- 2,391 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A077EA44
- Ligands
- SO4
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 394 | — | A0A077EA44 |
| B | — | protein | 441 | — | A0A077EA44 |
| C, D, E, F | — | protein | 389 | — | A0A077EA44 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 44 copies · chains A, B, D, C, E, F
- CIT · Citric acid · additive · 6 copies · chains A, B, C, E, D, F
- EDO · 1,2-ethanediol · additive · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7N7S · Crystal Structure of Hydroxymethylglutaryl-CoA reductase from Elizabethkingia anophelis… · 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 A0A077EA44
- Elsewhere: RCSB PDB 7N7S · PDBe 7N7S · UniProt A0A077EA44
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