Research workbench
Crystal structure analysis of the mini-chaperonines, variant with gly 184 replaced with ile and leu 185 replaced val and val 186 replaced with leu.
Analyse Crystal structure analysis of the mini-chaperonines, variant with gly 184… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3VZ6
- Type
- protein
- Length
- 193 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 60 kda chaperonin
- UniProt
- P0A6F5
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 60 kda chaperonin | protein | 193 | 45% helix, 23% strand | P0A6F5 |
Compared structures
- 3VZ6 · Crystal Structure Analysis of the Mini-chaperonines, variant with Gly 184 replaced with… · the same entry in another collection · chain A against A, TM-score 1.00
- P0A6F5 · AlphaFold monomer V2.0 prediction for 60 kda chaperonin (P0A6F5) · 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 P0A6F5
- Elsewhere: RCSB PDB 3VZ6 · PDBe 3VZ6 · UniProt P0A6F5
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