Research workbench
Crystal structure of the irre protein, a central regulator of DNA damage repair in deinococcaceae
Analyse Crystal structure of the irre protein, a central regulator of DNA damage repair… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3DTK
- Type
- protein
- Length
- 247 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Irre protein
- UniProt
- B5B9W8
- Ligands
- ZN, CL
- Pockets
- 1 · best druggability 0.47
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Irre protein | protein | 247 | 43% helix, 21% strand | B5B9W8 |
Ligands and binding sites
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 | 143 | 0.47 | 0.77 | 21 | empty |
Compared structures
- 3DTK · Crystal structure of the IRRE protein, a central regulator of DNA damage repair in… · 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 B5B9W8
- Elsewhere: RCSB PDB 3DTK · PDBe 3DTK · UniProt B5B9W8
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