Research workbench
Crystal structure of C. elegans erh-2 pid-3 complex
Analyse Crystal structure of C. elegans erh-2 pid-3 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7O6N
- Type
- protein
- Length
- 224 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Enhancer of rudimentary homolog 2; Protein pid-3
- UniProt
- Q20057, O76616
Structure
x-ray diffraction · 4 distinct chains · 50% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Enhancer of rudimentary homolog 2 | protein | 95 | 47% helix, 26% strand | Q20057 |
| B | Enhancer of rudimentary homolog 2 | protein | 97 | 45% helix, 26% strand | Q20057 |
| C | Protein pid-3 | protein | 17 | 71% helix, 0% strand | O76616 |
| D | Protein pid-3 | protein | 15 | 73% helix, 0% strand | O76616 |
Ligands and binding sites
- FMT · Formic acid · additive · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
5 interfaces between chains.
- A–B · 748 Ų buried · 15 hydrogen bonds · protein-protein
- B–C · 622 Ų buried · 5 hydrogen bonds · protein-protein
- A–D · 562 Ų buried · 3 hydrogen bonds · protein-protein
- A–C · 153 Ų buried · 3 hydrogen bonds · protein-protein
- B–D · 153 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 7O6N · Crystal structure of C. elegans ERH-2 PID-3 complex · the same entry in another collection · chain D against D, TM-score 1.00
- Q20057 · AlphaFold monomer V2.0 prediction for enhancer of rudimentary homolog 2 (Q20057) · a predicted model of the same protein · chain B against A, TM-score 0.92
- O76616 · AlphaFold monomer V2.0 prediction for protein pid-3 (O76616) · a predicted model of the same protein · chain D against A, TM-score 0.67
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 Q20057
- Every structure of UniProt O76616
- Elsewhere: RCSB PDB 7O6N · PDBe 7O6N · UniProt Q20057 · UniProt O76616
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