Research workbench
Crystal structure of domain 2 of thermotoga maritima N-utilization substance G (nusg)
Analyse Crystal structure of domain 2 of thermotoga maritima N-utilization substance G… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2XHA
- Type
- protein
- Length
- 386 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcription antitermination protein nusg
- UniProt
- P29397
- Pockets
- 4 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 3% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Transcription antitermination protein nusg | protein | 193 | 3% helix, 47% strand | P29397 |
Ligands and binding sites
- ACT · Acetate ion · additive · 7 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 720 | 0.81 | 0.85 | 84 | ACT |
| 2 | 370 | 0.77 | 0.87 | 53 | ACT |
| 3 | 80 | 0.34 | 0.75 | 15 | empty |
| 4 | 62 | 0.29 | 0.74 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 712 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 2XHA · Crystal Structure of Domain 2 of Thermotoga maritima N-utilization Substance G (NusG) · the same entry in another collection · chain A against A, TM-score 1.00
- P29397 · AlphaFold monomer V2.0 prediction for transcription TERMINATION/ANTITERMINATION protein… · a predicted model of the same protein · chain A against A, TM-score 0.94
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 P29397
- Elsewhere: RCSB PDB 2XHA · PDBe 2XHA · UniProt P29397
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