Research workbench
Crystal structure analysis of the radixin ferm domain complexed with adhesion molecule CD43
Analyse Crystal structure analysis of the radixin ferm domain complexed with adhesion… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2EMS
- Type
- protein
- Length
- 331 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Radixin; Leukosialin
- UniProt
- P26043, P15702
- Pockets
- 6 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Radixin | protein | 316 | 38% helix, 24% strand | P26043 |
| B | Leukosialin | protein | 15 | 0% helix, 27% strand | P15702 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 622 | 0.70 | 0.78 | 61 | empty |
| 2 | 117 | 0.51 | 0.81 | 17 | empty |
| 3 | 67 | 0.41 | 0.80 | 12 | empty |
| 4 | 64 | 0.33 | 0.77 | 19 | empty |
| 5 | 80 | 0.31 | 0.73 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 620 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 2EMS · Crystal Structure Analysis of the radixin FERM domain complexed with adhesion molecule… · the same entry in another collection · chain B against B, TM-score 1.00
- P26043 · AlphaFold monomer V2.0 prediction for radixin (P26043) · a predicted model of the same protein · chain A against A, TM-score 0.96
- P15702 · AlphaFold monomer V2.0 prediction for leukosialin (P15702) · a predicted model of the same protein · chain B against A, TM-score 0.25
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 P26043
- Every structure of UniProt P15702
- Elsewhere: RCSB PDB 2EMS · PDBe 2EMS · UniProt P26043 · UniProt P15702
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