Research workbench
Crystal structure of human NDRG2 protein provides insight into its role as a tumor suppressor
Analyse Crystal structure of human NDRG2 protein provides insight into its role as a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2XMS
- Type
- protein
- Length
- 281 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein NDRG2
- UniProt
- Q9UN36
- Ligands
- CL
- Pockets
- 2 · best druggability 0.47
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein NDRG2 | protein | 281 | 43% helix, 18% strand | Q9UN36 |
Ligands and binding sites
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 | 192 | 0.47 | 0.75 | 23 | empty |
| 2 | 96 | 0.36 | 0.74 | 21 | IMD |
Compared structures
- 2XMS · Crystal structure of human NDRG2 protein provides insight into its role as a tumor… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9UN36 · AlphaFold monomer V2.0 prediction for protein NDRG2 (Q9UN36) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q9UN36
- Elsewhere: RCSB PDB 2XMS · PDBe 2XMS · UniProt Q9UN36
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