MolNFT v1 · #17080 · protein
Peptidoglycan recognition protein-lb
1OHT · CG14704 protein: “Peptidoglycan recognition protein-lb”. X-ray diffraction, 1 ligand (ZN), 1 pocket (best druggability 0.32). MolNFT v1 #17080 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1OHT
- Type
- protein
- Length
- 173 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CG14704 protein
- UniProt
- Q9VGN3
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.32
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CG14704 protein | protein | 173 | 29% helix, 20% strand | Q9VGN3 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
- EDO · 1,2-ethanediol · additive · 2 copies · chains A
- TLA · L(+)-tartaric acid · additive · 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 82 | 0.32 | 0.73 | 16 | ZN |
Modifications
Observed in the structure: 6 modified, 1 disulfide (engineered, disulfide).
Compared structures
- 1OHT · Peptidoglycan recognition protein LB · 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 Q9VGN3
- Elsewhere: RCSB PDB 1OHT · PDBe 1OHT · UniProt Q9VGN3
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