Research workbench
Crystal structure of citrus MAF1 in space group C 2 2 21
Analyse Crystal structure of citrus MAF1 in space group C 2 2 21 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5U50
- Type
- protein
- Length
- 680 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Repressor of RNA polymerase III transcription
- UniProt
- G9I821
- Pockets
- 6 · best druggability 0.62
Structure
x-ray diffraction · 4 distinct chains · 46% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Repressor of RNA polymerase III transcription | protein | 178 | 45% helix, 24% strand | G9I821 |
| B | Repressor of RNA polymerase III transcription | protein | 172 | 47% helix, 26% strand | G9I821 |
| C | Repressor of RNA polymerase III transcription | protein | 167 | 45% helix, 25% strand | G9I821 |
| D | Repressor of RNA polymerase III transcription | protein | 163 | 49% helix, 26% strand | G9I821 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 70 | 0.62 | 0.91 | 23 | empty |
| 2 | 166 | 0.51 | 0.78 | 26 | empty |
| 3 | 168 | 0.44 | 0.74 | 34 | empty |
| 4 | 116 | 0.43 | 0.77 | 22 | empty |
| 5 | 90 | 0.39 | 0.77 | 22 | empty |
Interfaces
3 interfaces between chains.
- A–B · 973 Ų buried · 14 hydrogen bonds · protein-protein
- C–D · 742 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 678 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 5U50 · Crystal structure of citrus MAF1 in space group C 2 2 21 · the same entry in another collection · chain A against A, TM-score 1.00
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 G9I821
- Elsewhere: RCSB PDB 5U50 · PDBe 5U50 · UniProt G9I821
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