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Crystal structure of human RNA-binding protein 12
Analyse Crystal structure of human RNA-binding protein 12 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2EK6
- Type
- protein
- Length
- 312 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RNA-binding protein 12
- UniProt
- Q9NTZ6
- Pockets
- 4 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 23% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | RNA-binding protein 12 | protein | 78 | 23% helix, 33% strand | Q9NTZ6 |
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 | 123 | 0.79 | 0.97 | 30 | empty |
| 2 | 70 | 0.53 | 0.86 | 18 | empty |
| 3 | 147 | 0.41 | 0.74 | 33 | empty |
| 4 | 108 | 0.36 | 0.73 | 24 | empty |
Interfaces
6 interfaces between chains.
- A–B · 623 Ų buried · 5 hydrogen bonds · protein-protein
- C–D · 575 Ų buried · 7 hydrogen bonds · protein-protein
- A–D · 437 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 389 Ų buried · 3 hydrogen bonds · protein-protein
- B–D · 356 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
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 Q9NTZ6
- Elsewhere: RCSB PDB 2EK6 · PDBe 2EK6 · UniProt Q9NTZ6
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