MolNFT v1 · #38450 · protein
Crystal structure of human artemin
2GYR · Neurotrophic factor artemin, isoform 3: “Crystal structure of human artemin”. X-ray diffraction, 5 pockets (best druggability 0.77). MolNFT v1 #38450 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2GYR
- Type
- protein
- Length
- 582 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Neurotrophic factor artemin, isoform 3
- UniProt
- Q5T4W7
- Pockets
- 5 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 16% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Neurotrophic factor artemin, isoform 3 | protein | 97 | 16% helix, 41% strand | Q5T4W7 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 807 | 0.77 | 0.81 | 74 | empty |
| 2 | 161 | 0.41 | 0.74 | 28 | empty |
| 3 | 86 | 0.36 | 0.76 | 25 | empty |
| 4 | 76 | 0.36 | 0.77 | 27 | empty |
| 5 | 68 | 0.27 | 0.72 | 14 | empty |
Interfaces
9 interfaces between chains.
- C–D · 1667 Ų buried · 25 hydrogen bonds · protein-protein
- E–F · 1661 Ų buried · 29 hydrogen bonds · protein-protein
- A–B · 1654 Ų buried · 29 hydrogen bonds · protein-protein
- C–E · 197 Ų buried · 1 hydrogen bond · protein-protein
- D–E · 133 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 21 disulfide (disulfide).
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 Q5T4W7
- Elsewhere: RCSB PDB 2GYR · PDBe 2GYR · UniProt Q5T4W7
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