Research workbench
Udp glucose alpha tetrahydrobiopterin glycosyltransferase from synechococcus species pcc 7942 - BH2 complex form
Analyse Udp glucose alpha tetrahydrobiopterin glycosyltransferase from synechococcus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5ZER
- Type
- protein
- Length
- 700 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Udp-GLUCOSE:TETRAHYDROBIOPTERIN glucosyltransferase
- UniProt
- Q93EY3
- Ligands
- HBI
- Pockets
- 7 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-GLUCOSE:TETRAHYDROBIOPTERIN glucosyltransferase | protein | 354 | 39% helix, 17% strand | Q93EY3 |
| B | Udp-GLUCOSE:TETRAHYDROBIOPTERIN glucosyltransferase | protein | 346 | 35% helix, 15% strand | Q93EY3 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 957 | 0.82 | 0.83 | 90 | HBI |
| 2 | 935 | 0.75 | 0.78 | 80 | HBI |
| 3 | 70 | 0.69 | 0.95 | 20 | GOL |
| 4 | 145 | 0.63 | 0.86 | 26 | empty |
| 5 | 133 | 0.62 | 0.86 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 1030 Ų buried · 19 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 5ZER · UDP Glucose alpha tetrahydrobiopterin glycosyltransferase from Synechococcus species PCC… · 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 Q93EY3
- Elsewhere: RCSB PDB 5ZER · PDBe 5ZER · UniProt Q93EY3
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