Research workbench
Crystal structure of human growth and differentiation factor 5 (gdf-5)
Analyse Crystal structure of human growth and differentiation factor 5 (gdf-5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1WAQ
- Type
- protein
- Length
- 104 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GROWTH/DIFFERENTIATION factor 5
- UniProt
- P43026
Structure
x-ray diffraction · 1 distinct chain · 14% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GROWTH/DIFFERENTIATION factor 5 | protein | 104 | 14% helix, 45% strand | P43026 |
Ligands and binding sites
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 1WAQ · Crystal structure of human Growth and Differentiation Factor 5 (GDF-5) · the same entry in another collection · chain A against A, TM-score 1.00
- P43026 · AlphaFold monomer V2.0 prediction for GROWTH/DIFFERENTIATION factor 5 (P43026) · a predicted model of the same protein · chain A against A, TM-score 0.93
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 P43026
- Elsewhere: RCSB PDB 1WAQ · PDBe 1WAQ · UniProt P43026
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.