MolNFT v1 · #187272 · protein
Crystal structure of the EPHB2 extracellular domain
7S7K · Ephrin type-B receptor 2: “Crystal structure of the EPHB2 extracellular domain”. X-ray diffraction, 2 ligands (NAG, BMA), 1 pocket (best druggability 0.40). MolNFT v1 #187272 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 7S7K
- Type
- protein
- Length
- 525 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ephrin type-B receptor 2
- EC
- 2.7.10.1
- UniProt
- P54763
- Ligands
- NAG, BMA
- Pockets
- 1 · best druggability 0.40
Structure
x-ray diffraction · 1 distinct chain · 4% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ephrin type-B receptor 2 (EC 2.7.10.1) | protein | 525 | 4% helix, 45% strand | P54763 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 6 copies · chains A
- BMA · beta-D-mannopyranose · sugar
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 | 117 | 0.40 | 0.75 | 23 | empty |
Modifications
Observed in the structure: 10 disulfide, 4 glycan (disulfide, N-glycosylation).
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 P54763
- Elsewhere: RCSB PDB 7S7K · PDBe 7S7K · UniProt P54763
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