Research workbench
Crystal structure of VEGFR-3 extracellular domains D4-5
Analyse Crystal structure of VEGFR-3 extracellular domains D4-5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4BSJ
- Type
- protein
- Length
- 213 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.5
- Source
- HOMO SAPIENS
- Molecule
- Vascular endothelial growth factor receptor 3
- EC
- 2.7.10.1
- UniProt
- P35916
- Ligands
- NAG
Structure
x-ray diffraction · resolution 2.5 · 1 distinct chain · 3% helix, 58% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vascular endothelial growth factor receptor 3 (EC 2.7.10.1) | protein | 213 | 3% helix, 58% strand | P35916 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 2 disulfide, 2 glycan (disulfide, N-glycosylation).
Compared structures
- 4BSJ · Crystal structure of vegfr-3 extracellular domains D4-5 · the same entry in another collection · chain A against A, TM-score 1.00
- P35916 · AlphaFold monomer V2.0 prediction for vascular endothelial growth factor receptor 3… · a predicted model of the same protein · chain A against A, TM-score 0.91
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 P35916
- Elsewhere: RCSB PDB 4BSJ · PDBe 4BSJ · UniProt P35916
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