MolNFT v2 · #168012 · protein
Crystal structure of Z032 Fab in complex with WNV EDIII
6UTE: “Crystal structure of Z032 Fab in complex with WNV EDIII”. X-ray diffraction at 2.9. MolNFT v2 #168012 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6UTE
- Type
- protein
- Length
- 2,269 residues
- Chains
- 11
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.9
- Source
- Homo sapiens; West Nile virus
- UniProt
- S6B291, P0DOX7, Q06C97
Structure
x-ray diffraction · resolution 2.9 · 7 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | — | protein | 219 | — | S6B291 |
| D, B, F, J | — | protein | 213 | — | P0DOX7 |
| S | — | protein | 98 | — | Q06C97 |
| A, G | — | protein | 223 | — | S6B291 |
| E | — | protein | 220 | — | S6B291 |
| H | — | protein | 210 | — | P0DOX7 |
| I | — | protein | 224 | — | S6B291 |
Ligands and binding sites
- GOL · Glycerol · additive · 5 copies · chains C, D, B, E, F, I, J
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
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 S6B291
- Every structure of UniProt P0DOX7
- Every structure of UniProt Q06C97
- Elsewhere: RCSB PDB 6UTE · PDBe 6UTE · UniProt S6B291 · UniProt P0DOX7 · UniProt Q06C97
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