MolNFT v1 · #148175 · protein
Human butyrylcholinesterase carbamylated.
6EZ2: “Human butyrylcholinesterase carbamylated.”. X-ray diffraction, 2 ligands (NAG, CL). MolNFT v1 #148175 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6EZ2
- Type
- protein
- Length
- 1,052 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P06276
- Ligands
- NAG, CL
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 527 | — | P06276 |
| B | — | protein | 525 | — | P06276 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 15 copies · chains A, B
- CL · Chloride ion · ion · chains A
- GOL · Glycerol · additive · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 2 copies · chains B
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 P06276
- Elsewhere: RCSB PDB 6EZ2 · PDBe 6EZ2 · UniProt P06276
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