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Crystal structure of beta-hexosyl transferase from hamamotoa (sporobolomyces) singularis bound to tris
Analyse Crystal structure of beta-hexosyl transferase from hamamotoa (sporobolomyces)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7L74
- Type
- protein
- Length
- 1,083 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-hexosyltransferase
- UniProt
- Q564N5
- Ligands
- NAG, CA
- Pockets
- 3 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-hexosyltransferase | protein | 541 | 45% helix, 11% strand | Q564N5 |
| B | Beta-hexosyltransferase | protein | 542 | 45% helix, 11% strand | Q564N5 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 16 copies · chains A, B
- CA · Calcium ion · metal · chains A, B
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 399 | 0.77 | 0.86 | 52 | empty |
| 2 | 597 | 0.70 | 0.78 | 60 | TRS |
| 3 | 548 | 0.69 | 0.78 | 60 | TRS |
Interfaces
1 interface between chains.
- A–B · 1644 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 glycan, 6 disulfide, 6 modified (N-glycosylation, disulfide, phosphorylation).
Compared structures
- 7L74 · Crystal structure of Beta-hexosyl transferase from Hamamotoa (Sporobolomyces) singularis… · 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 Q564N5
- Elsewhere: RCSB PDB 7L74 · PDBe 7L74 · UniProt Q564N5
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