Research workbench
Molecular architectures of the 24MERIC eye lens chaperone alphab- crystallin elucidated by a triple hybrid approach
Analyse Molecular architectures of the 24MERIC eye lens chaperone alphab- crystallin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2YGD
- Type
- protein
- Length
- 4,200 residues
- Chains
- 24
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-crystallin B chain
- UniProt
- P02511
- Pockets
- 20 · best druggability 0.77
Structure
electron microscopy · 1 distinct chain · 14% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X | Alpha-crystallin B chain | protein | 175 | 14% helix, 29% strand | P02511 |
Pockets
20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 97 | 0.77 | 0.98 | 30 | empty |
| 2 | 88 | 0.76 | 0.97 | 22 | empty |
| 3 | 80 | 0.75 | 0.98 | 28 | empty |
| 4 | 72 | 0.74 | 0.98 | 26 | empty |
| 5 | 113 | 0.68 | 0.91 | 30 | empty |
Interfaces
72 interfaces between chains.
- O–P · 2807 Ų buried · 44 hydrogen bonds · protein-protein
- U–V · 2804 Ų buried · 44 hydrogen bonds · protein-protein
- S–T · 2802 Ų buried · 46 hydrogen bonds · protein-protein
- M–N · 2800 Ų buried · 45 hydrogen bonds · protein-protein
- C–D · 2799 Ų buried · 44 hydrogen bonds · protein-protein
Compared structures
- 2YGD · Molecular architectures of the 24meric eye lens chaperone alphaB- crystallin elucidated… · the same entry in another collection · chain K against K, TM-score 1.00
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 P02511
- Elsewhere: RCSB PDB 2YGD · PDBe 2YGD · UniProt P02511
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