MolNFT v1 · #117311 · protein
Crystal structure of human growth differentiation factor 11 (gdf-11)
5E4G · GROWTH/DIFFERENTIATION factor 11: “Crystal structure of human growth differentiation factor 11 (gdf-11)”. X-ray diffraction. MolNFT v1 #117311 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5E4G
- Type
- protein
- Length
- 108 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GROWTH/DIFFERENTIATION factor 11
- UniProt
- O95390
Structure
x-ray diffraction · 1 distinct chain · 7% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GROWTH/DIFFERENTIATION factor 11 | protein | 108 | 7% helix, 44% strand | O95390 |
Ligands and binding sites
- PG4 · Tetraethylene glycol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 5E4G · Crystal structure of human growth differentiation factor 11 (GDF-11) · the same entry in another collection · chain A against A, TM-score 1.00
- O95390 · AlphaFold monomer V2.0 prediction for GROWTH/DIFFERENTIATION factor 11 (O95390) · a predicted model of the same protein · chain A against A, TM-score 0.79
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 O95390
- Elsewhere: RCSB PDB 5E4G · PDBe 5E4G · UniProt O95390
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