Research workbench
Crystal structure of the ZNF4 of nucleoporin NUP153 in complex with ran-GDP
Analyse Crystal structure of the ZNF4 of nucleoporin NUP153 in complex with ran-GDP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7MO5
- Type
- protein
- Length
- 238 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GTP-binding nuclear protein ran; Nuclear pore complex protein NUP153
- UniProt
- P62826, P49791
- Ligands
- GDP, MG, ZN
- Pockets
- 1 · best druggability 0.41
Structure
x-ray diffraction · 2 distinct chains · 28% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GTP-binding nuclear protein ran | protein | 202 | 33% helix, 27% strand | P62826 |
| B | Nuclear pore complex protein NUP153 | protein | 36 | 0% helix, 17% strand | P49791 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · chains A
- MG · Magnesium ion · metal · chains A
- ZN · Zinc ion · metal · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 72 | 0.41 | 0.80 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 723 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 7MO5 · Crystal Structure of the ZnF4 of Nucleoporin NUP153 in complex with Ran-GDP · the same entry in another collection · chain A against A, TM-score 1.00
- P49791 · AlphaFold monomer V2.0 prediction for nuclear pore complex protein NUP153 (P49791) · a predicted model of the same protein · chain B 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 P62826
- Every structure of UniProt P49791
- Elsewhere: RCSB PDB 7MO5 · PDBe 7MO5 · UniProt P62826 · UniProt P49791
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