MolNFT v1 · #135119 · protein
Crystal structure of a de novo designed protein homodimer with curved beta-sheet
5TPH · De novo NTF2 homodimer: “Crystal structure of a de novo designed protein homodimer with curved beta-sheet”. X-ray diffraction, 1 ligand (CL), 4 pockets (best druggability 0.71). MolNFT v1 #135119 on GenesisL1: 3D structure, binding…
- PDB
- 5TPH
- Type
- protein
- Length
- 241 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- De novo NTF2 homodimer
- Ligands
- CL
- Pockets
- 4 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | De novo NTF2 homodimer | protein | 120 | 37% helix, 44% strand | — |
| B | De novo NTF2 homodimer | protein | 121 | 36% helix, 45% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 298 | 0.71 | 0.84 | 42 | PEG |
| 2 | 169 | 0.52 | 0.79 | 30 | empty |
| 3 | 88 | 0.38 | 0.76 | 14 | empty |
| 4 | 98 | 0.37 | 0.75 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1026 Ų buried · 6 hydrogen bonds · protein-protein
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 5TPH · PDBe 5TPH
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