MolNFT v1 · #94247 · protein
Crystal structure of the pneumoccocal exposed lipoprotein thioredoxin SP_1000 (ETRX2) from streptococcus pneumoniae strain TIGR4 in complex with 2-hydroxyethyl disulfide
4HQZ · Thioredoxin family protein: “Crystal structure of the pneumoccocal exposed lipoprotein thioredoxin SP_1000 (ETRX2) from streptococcus…”. X-ray diffraction, 4 pockets (best druggability 0.38). MolNFT v1 #94247 on GenesisL1: 3D…
- PDB
- 4HQZ
- Type
- protein
- Length
- 286 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thioredoxin family protein
- UniProt
- Q97R36
- Pockets
- 4 · best druggability 0.38
Structure
x-ray diffraction · 2 distinct chains · 28% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thioredoxin family protein | protein | 141 | 28% helix, 26% strand | Q97R36 |
| B | Thioredoxin family protein | protein | 145 | 28% helix, 25% strand | Q97R36 |
Ligands and binding sites
- HED · 2-hydroxyethyl disulfide · additive · 2 copies · chains A, B
- PEG · Di(hydroxyethyl)ether · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 64 | 0.38 | 0.78 | 14 | HED |
| 2 | 69 | 0.37 | 0.78 | 15 | HED |
| 3 | 61 | 0.37 | 0.79 | 18 | empty |
| 4 | 83 | 0.36 | 0.75 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 617 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 4HQZ · Crystal structure of the pneumoccocal exposed lipoprotein thioredoxin sp_1000 (Etrx2)… · 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 Q97R36
- Elsewhere: RCSB PDB 4HQZ · PDBe 4HQZ · UniProt Q97R36
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