Research workbench
Crystal structure of the gld-1 homodimerization domain from caenorhabditis elegans at 2.04 a resolution
Analyse Crystal structure of the gld-1 homodimerization domain from caenorhabditis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3K6T
- Type
- protein
- Length
- 203 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q17339
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 54 | — | Q17339 |
| B | — | protein | 49 | — | Q17339 |
| D | — | protein | 46 | — | Q17339 |
Compared structures
- 3K6T · Crystal structure of the GLD-1 homodimerization domain from Caenorhabditis elegans at… · the same entry in another collection · chain D against D, TM-score 1.00
- Q17339 · AlphaFold monomer V2.0 prediction for female germline-specific tumor suppressor gld-1… · a predicted model of the same protein · chain D against A, TM-score 0.90
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 Q17339
- Elsewhere: RCSB PDB 3K6T · PDBe 3K6T · UniProt Q17339
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