MolNFT v1 · #65938 · protein
Crystal structure pseg-udp complex from campylobacter jejuni
3HBN · Udp-sugar hydrolase: “Crystal structure pseg-udp complex from campylobacter jejuni”. X-ray diffraction, 2 ligands (UDP, CL), 1 pocket (best druggability 0.77). MolNFT v1 #65938 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 3HBN
- Type
- protein
- Length
- 282 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Udp-sugar hydrolase
- UniProt
- Q0P8U5
- Ligands
- UDP, CL
- Pockets
- 1 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-sugar hydrolase | protein | 282 | 34% helix, 23% strand | Q0P8U5 |
Ligands and binding sites
- UDP · Uridine-5'-diphosphate · ligand · chains A
- CL · Chloride ion · ion · chains A
- GOL · Glycerol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 503 | 0.77 | 0.85 | 61 | UDP, GOL, CL |
Modifications
Observed in the structure: 3 modified (engineered).
Compared structures
- 3HBN · Crystal structure PseG-UDP complex from Campylobacter jejuni · the same entry in another collection · chain A against A, TM-score 1.00
- Q0P8U5 · AlphaFold monomer V2.0 prediction for udp-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyran… · 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 Q0P8U5
- Elsewhere: RCSB PDB 3HBN · PDBe 3HBN · UniProt Q0P8U5
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