Research workbench
Pseudo-atomic model of a 16-mer assembly of reduced recombinant human alphaa-crystallin (non domain swapped configuration)
Analyse Pseudo-atomic model of a 16-mer assembly of reduced recombinant human… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6T1R
- Type
- protein
- Length
- 2,656 residues
- Chains
- 16
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-crystallin a chain
- UniProt
- P02489
- Pockets
- 20 · best druggability 0.61
Structure
electron microscopy · 1 distinct chain · 4% helix, 27% 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 | Alpha-crystallin a chain | protein | 166 | 4% helix, 27% strand | P02489 |
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 | 306 | 0.61 | 0.79 | 52 | empty |
| 2 | 329 | 0.60 | 0.77 | 54 | empty |
| 3 | 276 | 0.56 | 0.77 | 45 | empty |
| 4 | 246 | 0.55 | 0.77 | 41 | empty |
| 5 | 247 | 0.55 | 0.77 | 45 | empty |
Interfaces
24 interfaces between chains.
- I–J · 1577 Ų buried · 30 hydrogen bonds · protein-protein
- K–L · 1574 Ų buried · 30 hydrogen bonds · protein-protein
- C–D · 1572 Ų buried · 30 hydrogen bonds · protein-protein
- E–F · 1570 Ų buried · 29 hydrogen bonds · protein-protein
- M–N · 1569 Ų buried · 30 hydrogen bonds · protein-protein
Compared structures
- 6T1R · Pseudo-atomic model of a 16-mer assembly of reduced recombinant human alphaA-crystallin… · the same entry in another collection · chain O against O, 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 P02489
- Elsewhere: RCSB PDB 6T1R · PDBe 6T1R · UniProt P02489
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