MolNFT v1 · #143599 · protein
Crystal structure of human GLE1 ctd-NUP42 gbm complex
6B4F · Nucleoporin GLE1: “Crystal structure of human GLE1 ctd-NUP42 gbm complex”. X-ray diffraction, 2 ligands (PO4, CL), 11 pockets (best druggability 0.64). MolNFT v1 #143599 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6B4F
- Type
- protein
- Length
- 718 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nucleoporin GLE1; Nucleoporin like 2
- UniProt
- Q53GS7, Q3B7J4
- Ligands
- PO4, CL
- Pockets
- 11 · best druggability 0.64
Structure
x-ray diffraction · 3 distinct chains · 64% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Nucleoporin GLE1 | protein | 315 | 66% helix, 2% strand | Q53GS7 |
| A | Nucleoporin GLE1 | protein | 313 | 68% helix, 2% strand | Q53GS7 |
| C, D | Nucleoporin like 2 | protein | 45 | 24% helix, 0% strand | Q3B7J4 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 2 copies · chains B, A
- CL · Chloride ion · ion · 2 copies · chains A, D, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 428 | 0.64 | 0.77 | 53 | empty |
| 2 | 259 | 0.58 | 0.78 | 31 | PO4 |
| 3 | 142 | 0.56 | 0.82 | 16 | CL |
| 4 | 127 | 0.53 | 0.81 | 16 | CL |
| 5 | 161 | 0.42 | 0.74 | 24 | empty |
Interfaces
5 interfaces between chains.
- B–C · 1366 Ų buried · 24 hydrogen bonds · protein-protein
- A–D · 1322 Ų buried · 13 hydrogen bonds · protein-protein
- B–A · 958 Ų buried · 14 hydrogen bonds · protein-protein
- A–C · 67 Ų buried · 0 hydrogen bonds · protein-protein
- B–D · 57 Ų buried · 0 hydrogen bonds · protein-protein
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 Q53GS7
- Every structure of UniProt Q3B7J4
- Elsewhere: RCSB PDB 6B4F · PDBe 6B4F · UniProt Q53GS7 · UniProt Q3B7J4
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