Research workbench
Crystal structure of ggcgt in complex with udp-glu
Analyse Crystal structure of ggcgt in complex with udp-glu in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6L5S
- Type
- protein
- Length
- 454 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ggcgt
- Ligands
- UDP, G50
- Pockets
- 5 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ggcgt | protein | 454 | 49% helix, 15% strand | — |
Ligands and binding sites
- UDP · Uridine-5'-diphosphate · ligand · chains A
- G50 · 3-(4-hydroxyphenyl)-1-(2,4,6-trihydroxyphenyl)propan-1-one · ligand · chains A
- GOL · Glycerol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 580 | 0.86 | 0.91 | 61 | UDP, G50, GOL |
| 2 | 104 | 0.36 | 0.74 | 23 | empty |
| 3 | 55 | 0.32 | 0.76 | 15 | empty |
| 4 | 51 | 0.30 | 0.76 | 13 | empty |
| 5 | 59 | 0.27 | 0.73 | 19 | empty |
Compared structures
- 6L5S · crystal structure of GgCGT in complex with UDP-Glu · 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
- Elsewhere: RCSB PDB 6L5S · PDBe 6L5S
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