MolNFT v1 · #62316 · protein
Refinement at 1.4 ångströms resolution of a model of erabutoxin B. treatment of ordered solvent and discrete disorder
3EBX: “Refinement at 1.4 ångströms resolution of a model of erabutoxin B. treatment of ordered solvent and discrete…”. X-ray diffraction, 1 ligand (SO4). MolNFT v1 #62316 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3EBX
- Type
- protein
- Length
- 62 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Erabutoxin B
- UniProt
- Q90VW1
- Ligands
- SO4
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Erabutoxin B | protein | 62 | 0% helix, 44% strand | Q90VW1 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 3EBX · Refinement at 1.4 ångströms resolution of a model of erabutoxin B. treatment of ordered… · the same entry in another collection · chain A against A, TM-score 1.00
- Q90VW1 · AlphaFold monomer V2.0 prediction for erabutoxin B (Q90VW1) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 Q90VW1
- Elsewhere: RCSB PDB 3EBX · PDBe 3EBX · UniProt Q90VW1
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