Research workbench
Crystal structure of DNA helicase repa in complex with sulfate at 1.95 a resolution
Analyse Crystal structure of DNA helicase repa in complex with sulfate at 1.95 a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1NLF
- Type
- protein
- Length
- 762 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Regulatory protein repa
- UniProt
- P20356
- Ligands
- SO4
- Pockets
- 8 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Regulatory protein repa | protein | 254 | 35% helix, 21% strand | P20356 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 416 | 0.69 | 0.81 | 58 | SO4 |
| 2 | 416 | 0.69 | 0.81 | 52 | SO4 |
| 3 | 57 | 0.43 | 0.83 | 13 | empty |
| 4 | 84 | 0.41 | 0.78 | 23 | empty |
| 5 | 52 | 0.38 | 0.80 | 15 | empty |
Interfaces
2 interfaces between chains.
- A–B · 1472 Ų buried · 23 hydrogen bonds · protein-protein
- B–C · 1460 Ų buried · 20 hydrogen bonds · protein-protein
Compared structures
- 1NLF · Crystal Structure of DNA Helicase RepA in complex with sulfate at 1.95 A resolution · the same entry in another collection · chain C against C, TM-score 1.00
- P20356 · AlphaFold monomer V2.0 prediction for regulatory protein repa (P20356) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P20356
- Elsewhere: RCSB PDB 1NLF · PDBe 1NLF · UniProt P20356
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