Research workbench
Crystal structure of uridine-diphospho-N-acetylglucosamine pyrophosphorylase from candida albicans, in the apo-like form
Analyse Crystal structure of uridine-diphospho-N-acetylglucosamine pyrophosphorylase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2YQC
- Type
- protein
- Length
- 480 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Udp-N-acetylglucosamine pyrophosphorylase
- EC
- 2.7.7.23
- UniProt
- O74933
- Ligands
- MG
- Pockets
- 5 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) | protein | 480 | 40% helix, 23% strand | O74933 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 569 | 0.63 | 0.75 | 64 | empty |
| 2 | 147 | 0.58 | 0.83 | 22 | empty |
| 3 | 260 | 0.58 | 0.78 | 29 | empty |
| 4 | 171 | 0.47 | 0.75 | 22 | empty |
| 5 | 53 | 0.40 | 0.82 | 15 | empty |
Compared structures
- 2YQC · Crystal Structure of uridine-diphospho-N-acetylglucosamine pyrophosphorylase from Candida… · the same entry in another collection · chain A against A, TM-score 1.00
- O74933 · AlphaFold monomer V2.0 prediction for udp-N-acetylglucosamine pyrophosphorylase (O74933) · a predicted model of the same protein · 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 O74933
- Elsewhere: RCSB PDB 2YQC · PDBe 2YQC · UniProt O74933
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