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Crystal structure of chaetomium thermophilum NUP145N apd
Analyse Crystal structure of chaetomium thermophilum NUP145N apd in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5HB5
- Type
- protein
- Length
- 279 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nucleoporin NUP145
- EC
- 3.4.21.-
- UniProt
- G0SAK3
- Pockets
- 2 · best druggability 0.32
Structure
x-ray diffraction · 2 distinct chains · 17% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleoporin NUP145 (EC 3.4.21.-) | protein | 139 | 17% helix, 29% strand | G0SAK3 |
| B | Nucleoporin NUP145 (EC 3.4.21.-) | protein | 140 | 17% helix, 29% strand | G0SAK3 |
Ligands and binding sites
- FLC · Citrate anion · additive · 7 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 72 | 0.32 | 0.74 | 20 | empty |
| 2 | 64 | 0.28 | 0.73 | 11 | empty |
Interfaces
1 interface between chains.
- A–B · 551 Ų buried · 5 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 G0SAK3
- Elsewhere: RCSB PDB 5HB5 · PDBe 5HB5 · UniProt G0SAK3
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