MolNFT v1 · #173669 · protein
The glucuronoyl esterase OTCE15A R268A variant from opitutus terrae in complex with, and covalently linked to, D-glucuronate
7B7H: “The glucuronoyl esterase OTCE15A R268A variant from opitutus terrae in complex with, and covalently linked…”. X-ray diffraction, 2 ligands (GCU, NA). MolNFT v1 #173669 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7B7H
- Type
- protein
- Length
- 374 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- B1ZMF4
- Ligands
- GCU, NA
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 374 | — | B1ZMF4 |
Ligands and binding sites
- GCU · alpha-D-glucopyranuronic acid · sugar · chains A
- NA · Sodium ion · metal · 2 copies · chains A
- EDO · 1,2-ethanediol · additive · 12 copies · chains A
- DMS · Dimethyl sulfoxide · additive · 11 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7B7H · The glucuronoyl esterase OtCE15A R268A variant from Opitutus terrae in complex with, and… · the same entry in another collection · chain A against A, TM-score 0.99
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 B1ZMF4
- Elsewhere: RCSB PDB 7B7H · PDBe 7B7H · UniProt B1ZMF4
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.