Research workbench
Crystal structure of crenezumab Fab
Analyse Crystal structure of crenezumab Fab in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5VZX
- Type
- protein
- Length
- 865 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0DOX5, Q0KKI6
- Ligands
- SO4
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| H, E | — | protein | 214 | — | P0DOX5 |
| L | — | protein | 218 | — | Q0KKI6 |
| I | — | protein | 219 | — | Q0KKI6 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 11 copies · chains H, L, E, I
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 2 copies · chains H, L, E, I
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 2 copies · chains L, I
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5VZX · Crystal structure of crenezumab Fab · the same entry in another collection · chain H against H, 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 P0DOX5
- Every structure of UniProt Q0KKI6
- Elsewhere: RCSB PDB 5VZX · PDBe 5VZX · UniProt P0DOX5 · UniProt Q0KKI6
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