MolNFT v2 · #116900 · protein
Thermobaculum terrenum O-GlcNAc hydrolase mutant - D120N
5DIY: “Thermobaculum terrenum O-GlcNAc hydrolase mutant - D120N”. X-ray diffraction at 2.06, 1 ligand (NAG). MolNFT v2 #116900 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5DIY
- Type
- protein
- Length
- 935 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.06
- Source
- Thermobaculum terrenum; SYNTHETIC CONSTRUCT
- UniProt
- Q15750, D1CDN2
- Ligands
- NAG
Structure
x-ray diffraction · resolution 2.06 · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| P, Q | — | protein | 5 | — | Q15750 |
| A | — | protein | 463 | — | D1CDN2 |
| B | — | protein | 462 | — | D1CDN2 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains P, A, Q, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5DIY · Thermobaculum terrenum O-glcnac hydrolase mutant - D120N · 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 Q15750
- Every structure of UniProt D1CDN2
- Elsewhere: RCSB PDB 5DIY · PDBe 5DIY · UniProt Q15750 · UniProt D1CDN2
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