Research workbench
Crystal structure of the erythrocyte spectrin tetramerization domain complex
Analyse Crystal structure of the erythrocyte spectrin tetramerization domain complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3LBX
- Type
- protein
- Length
- 322 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Spectrin alpha chain, erythrocyte; Spectrin beta chain, erythrocyte
- UniProt
- P02549, P11277
- Pockets
- 3 · best druggability 0.49
Structure
x-ray diffraction · 2 distinct chains · 84% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Spectrin alpha chain, erythrocyte | protein | 140 | 84% helix, 0% strand | P02549 |
| B | Spectrin beta chain, erythrocyte | protein | 182 | 85% helix, 0% strand | P11277 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 160 | 0.49 | 0.77 | 17 | empty |
| 2 | 161 | 0.48 | 0.77 | 23 | empty |
| 3 | 73 | 0.48 | 0.83 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1460 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 3LBX · Crystal Structure of the Erythrocyte Spectrin Tetramerization Domain Complex · the same entry in another collection · chain A against A, TM-score 1.00
- P11277 · AlphaFold monomer V2.0 prediction for spectrin beta chain, erythrocytic (P11277) · a predicted model of the same protein · chain B against A, TM-score 0.84
- P02549 · AlphaFold monomer V2.0 prediction for spectrin alpha chain, erythrocytic 1 (P02549) · a predicted model of the same protein · chain A 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 P02549
- Every structure of UniProt P11277
- Elsewhere: RCSB PDB 3LBX · PDBe 3LBX · UniProt P02549 · UniProt P11277
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