MolNFT v1 · #187975 · protein
P. aeruginosa lpxa in complex with ligand H16
7T5S · Acyl-[acyl-carrier-protein]--udp-N-acetylglucosamine O…: “P. aeruginosa lpxa in complex with ligand H16”. X-ray diffraction, 1 ligand (F3R), 20 pockets (best druggability 0.78). MolNFT v1 #187975 on GenesisL1: 3D structure, binding…
- PDB
- 7T5S
- Type
- protein
- Length
- 1,541 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acyl-[acyl-carrier-protein]--udp-N-acetylglucosamine O- acyltransferase
- EC
- 2.3.1.129
- UniProt
- A6V1E4
- Ligands
- F3R
- Pockets
- 20 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 18% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, D, E, F | Acyl-[acyl-carrier-protein]--udp-N-acetylglucosamine O- acyltransferase (EC 2.3.1.129) | protein | 257 | 18% helix, 28% strand | A6V1E4 |
| C | Acyl-[acyl-carrier-protein]--udp-N-acetylglucosamine O- acyltransferase (EC 2.3.1.129) | protein | 256 | 18% helix, 28% strand | A6V1E4 |
Ligands and binding sites
- F3R · N~2~-(cyclohexylacetyl)-N-1H-tetrazol-5-yl-L-alaninamide · ligand · 6 copies · chains A, B, C, D, F, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 910 | 0.78 | 0.81 | 92 | empty |
| 2 | 466 | 0.75 | 0.84 | 53 | F3R |
| 3 | 635 | 0.72 | 0.79 | 67 | F3R |
| 4 | 713 | 0.71 | 0.78 | 89 | F3R |
| 5 | 566 | 0.69 | 0.78 | 61 | F3R |
Interfaces
8 interfaces between chains.
- E–F · 1035 Ų buried · 10 hydrogen bonds · protein-protein
- A–C · 1028 Ų buried · 10 hydrogen bonds · protein-protein
- D–E · 1025 Ų buried · 13 hydrogen bonds · protein-protein
- B–C · 1013 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 1000 Ų buried · 13 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 A6V1E4
- Elsewhere: RCSB PDB 7T5S · PDBe 7T5S · UniProt A6V1E4
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