MolNFT v1 · #103080 · protein
Crystal structure of the chemokine binding protein from orf virus
4P5I: “Crystal structure of the chemokine binding protein from orf virus”. X-ray diffraction, 1 ligand (NAG), 3 pockets (best druggability 0.29). MolNFT v1 #103080 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4P5I
- Type
- protein
- Length
- 240 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chemokine binding protein
- UniProt
- Q2F862
- Ligands
- NAG
- Pockets
- 3 · best druggability 0.29
Structure
x-ray diffraction · 1 distinct chain · 13% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chemokine binding protein | protein | 240 | 13% helix, 40% strand | Q2F862 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 63 | 0.29 | 0.74 | 15 | empty |
| 2 | 50 | 0.29 | 0.76 | 17 | empty |
| 3 | 59 | 0.27 | 0.73 | 19 | NAG |
Modifications
Observed in the structure: 3 disulfide, 2 glycan (disulfide, N-glycosylation).
Compared structures
- 4P5I · Crystal structure of the chemokine binding protein from orf virus · 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 Q2F862
- Elsewhere: RCSB PDB 4P5I · PDBe 4P5I · UniProt Q2F862
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