MolNFT v1 · #191242 · protein
Crystal structure of bifunctional protein glmu from klebsiella pneumoniae subsp. pneumoniae
8CU9 · Bifunctional udp-N-acetylglucosamine…: “Crystal structure of bifunctional protein glmu from klebsiella pneumoniae subsp. pneumoniae”. X-ray diffraction, 1 ligand (CL), 2 pockets (best druggability 0.59). MolNFT v1 #191242 on…
- PDB
- 8CU9
- Type
- protein
- Length
- 451 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bifunctional udp-N-acetylglucosamine DIPHOSPHORYLASE/GLUCOSAMINE-1-phosphate…
- UniProt
- A0A8F6ZET2
- Ligands
- CL
- Pockets
- 2 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 22% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional udp-N-acetylglucosamine DIPHOSPHORYLASE/GLUCOSAMINE-1-phosphate N-acetyltransferase glmu | protein | 451 | 22% helix, 33% strand | A0A8F6ZET2 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 399 | 0.59 | 0.75 | 41 | empty |
| 2 | 187 | 0.46 | 0.75 | 25 | empty |
Compared structures
- 8CU9 · Crystal Structure of Bifunctional protein GlmU from Klebsiella pneumoniae subsp.… · 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 A0A8F6ZET2
- Elsewhere: RCSB PDB 8CU9 · PDBe 8CU9 · UniProt A0A8F6ZET2
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