Research workbench
Crystal structure of the trimerization domain of human EML4
Analyse Crystal structure of the trimerization domain of human EML4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4CGC
- Type
- protein
- Length
- 83 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Echinoderm microtubule-associated protein-like 4
- UniProt
- Q9HC35
Structure
x-ray diffraction · 3 distinct chains · 93% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Echinoderm microtubule-associated protein-like 4 | protein | 28 | 93% helix, 0% strand | Q9HC35 |
| B | Echinoderm microtubule-associated protein-like 4 | protein | 26 | 92% helix, 0% strand | Q9HC35 |
| C | Echinoderm microtubule-associated protein-like 4 | protein | 29 | 93% helix, 0% strand | Q9HC35 |
Interfaces
3 interfaces between chains.
- B–C · 616 Ų buried · 9 hydrogen bonds · protein-protein
- A–C · 593 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 578 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 modified (engineered).
Compared structures
- 4CGC · Crystal structure of the trimerization domain of human EML4 · the same entry in another collection · chain A against A, TM-score 1.00
- Q9HC35 · AlphaFold monomer V2.0 prediction for echinoderm microtubule- associated protein-like 4… · a predicted model of the same protein · chain A against A, TM-score 0.89
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 Q9HC35
- Elsewhere: RCSB PDB 4CGC · PDBe 4CGC · UniProt Q9HC35
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