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Crystal structure of lpxd from escherichia COLI
Analyse Crystal structure of lpxd from escherichia COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3EH0
- Type
- protein
- Length
- 1,023 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Udp-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase
- EC
- 2.3.1.-
- UniProt
- P21645
- Pockets
- 19 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 16% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Udp-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase (EC 2.3.1.-) | protein | 341 | 16% helix, 29% strand | P21645 |
Pockets
19 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 128 | 0.78 | 0.96 | 25 | empty |
| 2 | 97 | 0.77 | 0.98 | 37 | empty |
| 3 | 78 | 0.74 | 0.97 | 15 | empty |
| 4 | 539 | 0.65 | 0.76 | 54 | empty |
| 5 | 515 | 0.64 | 0.76 | 55 | empty |
Interfaces
3 interfaces between chains.
- B–C · 3088 Ų buried · 26 hydrogen bonds · protein-protein
- A–B · 3015 Ų buried · 30 hydrogen bonds · protein-protein
- A–C · 2864 Ų buried · 26 hydrogen bonds · protein-protein
Compared structures
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 P21645
- Elsewhere: RCSB PDB 3EH0 · PDBe 3EH0 · UniProt P21645
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