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Crystal structure of S.PNEUMONIAE N-acetylglucosamine-1-phosphate uridyltransferase, glmu, bound to acetyl coenzyme a
Analyse Crystal structure of S.PNEUMONIAE N-acetylglucosamine-1-phosphate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HM8
- Type
- protein
- Length
- 916 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Udp-N-acetylglucosamine-1-phosphate uridyltransferase
- EC
- 2.7.7.23
- UniProt
- Q97R46
- Ligands
- ACO, CA
- Pockets
- 3 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 24% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Udp-N-acetylglucosamine-1-phosphate uridyltransferase (EC 2.7.7.23) | protein | 458 | 24% helix, 31% strand | Q97R46 |
Ligands and binding sites
- ACO · Acetyl coenzyme *A · ligand · 2 copies · chains A, B
- CA · Calcium ion · metal · 4 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 406 | 0.60 | 0.76 | 43 | CA |
| 2 | 414 | 0.59 | 0.75 | 37 | CA |
| 3 | 50 | 0.26 | 0.74 | 12 | empty |
Compared structures
- 1HM8 · Crystal structure of S.PNEUMONIAE N-acetylglucosamine-1-phosphate uridyltransferase… · the same entry in another collection · chain A against A, TM-score 1.00
- Q97R46 · AlphaFold monomer V2.0 prediction for bifunctional protein glmu (Q97R46) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q97R46
- Elsewhere: RCSB PDB 1HM8 · PDBe 1HM8 · UniProt Q97R46
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