Research workbench
Serial femtosecond X-ray crystallography structure of ecr in complex with NADPH
Analyse Serial femtosecond X-ray crystallography structure of ecr in complex with NADPH in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6NA6
- Type
- protein
- Length
- 1,780 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative crotonyl-CoA reductase
- UniProt
- E4N096
- Ligands
- NDP
- Pockets
- 20 · best druggability 0.85
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, D, C | Putative crotonyl-CoA reductase | protein | 445 | 34% helix, 23% strand | E4N096 |
Ligands and binding sites
- NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · 4 copies · chains A, B, D, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 523 | 0.85 | 0.91 | 60 | empty |
| 2 | 556 | 0.84 | 0.90 | 75 | empty |
| 3 | 620 | 0.82 | 0.88 | 74 | empty |
| 4 | 637 | 0.82 | 0.86 | 54 | NDP |
| 5 | 548 | 0.81 | 0.88 | 63 | empty |
Interfaces
6 interfaces between chains.
- A–C · 1632 Ų buried · 25 hydrogen bonds · protein-protein
- B–D · 1616 Ų buried · 30 hydrogen bonds · protein-protein
- B–C · 1237 Ų buried · 18 hydrogen bonds · protein-protein
- A–D · 1196 Ų buried · 18 hydrogen bonds · protein-protein
- D–C · 998 Ų buried · 23 hydrogen bonds · protein-protein
Compared structures
- 6NA6 · Serial Femtosecond X-ray Crystallography Structure of ECR in complex with NADPH · the same entry in another collection · chain B against B, 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 E4N096
- Elsewhere: RCSB PDB 6NA6 · PDBe 6NA6 · UniProt E4N096
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