Research workbench
Heparin-binding domain from vascular endothelial growth factor, NMR, 20 structures
Analyse Heparin-binding domain from vascular endothelial growth factor, NMR, 20… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1VGH
- Type
- protein
- Length
- 55 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Vascular endothelial growth factor-165
- UniProt
- P15692
Structure
solution nmr · 1 distinct chain · 11% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vascular endothelial growth factor-165 | protein | 55 | 11% helix, 22% strand | P15692 |
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1VGH · Heparin-binding domain from vascular endothelial growth factor, NMR, 20 structures · the same entry in another collection · chain A against A, TM-score 1.00
- P15692 · AlphaFold monomer V2.0 prediction for vascular endothelial growth factor a (P15692) · a predicted model of the same protein · chain A against A, TM-score 0.72
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 P15692
- Elsewhere: RCSB PDB 1VGH · PDBe 1VGH · UniProt P15692
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