Research workbench
Crystal structure of the cap-gly domain of human dynactin-1 (P150- glued)
Analyse Crystal structure of the cap-gly domain of human dynactin-1 (P150- glued) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2HKN
- Type
- protein
- Length
- 148 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q14203
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 76 | — | Q14203 |
| B | — | protein | 72 | — | Q14203 |
Compared structures
- 2HKN · Crystal structure of the CAP-Gly domain of human Dynactin-1 (p150-Glued) · the same entry in another collection · chain B against B, TM-score 1.00
- Q14203 · AlphaFold monomer V2.0 prediction for dynactin subunit 1 (Q14203) · a predicted model of the same protein · chain B against A, TM-score 0.82
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 Q14203
- Elsewhere: RCSB PDB 2HKN · PDBe 2HKN · UniProt Q14203
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