Research workbench
X-ray crystal structure of a chemically synthesized [L-GLN35]UBIQUITIN with a cubic space group
Analyse X-ray crystal structure of a chemically synthesized [L-GLN35]UBIQUITIN with a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2FCS
- Type
- protein
- Length
- 146 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ubiquitin
- Ligands
- CD, SO4
Structure
x-ray diffraction · 1 distinct chain · 25% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Ubiquitin | protein | 73 | 25% helix, 34% strand | — |
Ligands and binding sites
- CD · Cadmium ion · metal · 7 copies · chains A, B
- SO4 · Sulfate ion · ion · chains A, B
- ACT · Acetate ion · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 455 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 2FCS · X-ray Crystal Structure of a Chemically Synthesized [L-Gln35]Ubiquitin with a Cubic Space… · 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
- Elsewhere: RCSB PDB 2FCS · PDBe 2FCS
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