Research workbench
Structure of the PHE2 and PHE3 fragments of the integrin BETA2 subunit
Analyse Structure of the PHE2 and PHE3 fragments of the integrin BETA2 subunit in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2P28
- Type
- protein
- Length
- 310 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Integrin beta-2
- UniProt
- P05107
- Ligands
- NAG
- Pockets
- 1 · best druggability 0.33
Structure
x-ray diffraction · 2 distinct chains · 10% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Integrin beta-2 | protein | 96 | 23% helix, 29% strand | P05107 |
| B | Integrin beta-2 | protein | 214 | 5% helix, 42% strand | P05107 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 54 | 0.33 | 0.77 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 2209 Ų buried · 37 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 17 disulfide (disulfide).
Compared structures
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 P05107
- Elsewhere: RCSB PDB 2P28 · PDBe 2P28 · UniProt P05107
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