MolNFT v1 · #58298 · protein
Beta-hydroxyacyl-acyl carrier protein dehydratase (fabz) from plasmodium falciparum in complex with NAS91
3AZ9 · Beta-hydroxyacyl-acp dehydratase: “Beta-hydroxyacyl-acyl carrier protein dehydratase (fabz) from plasmodium falciparum in complex with NAS91”. X-ray diffraction, 2 ligands (K91, PO4), 20 pockets (best druggability 0.83). MolNFT v1…
- PDB
- 3AZ9
- Type
- protein
- Length
- 3,468 residues
- Chains
- 24
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-hydroxyacyl-acp dehydratase
- EC
- 4.2.1.-
- UniProt
- Q965D7
- Ligands
- K91, PO4
- Pockets
- 20 · best druggability 0.83
Structure
x-ray diffraction · 8 distinct chains · 21% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, F, L, M, R, S | Beta-hydroxyacyl-acp dehydratase (EC 4.2.1.-) | protein | 146 | 21% helix, 41% strand | Q965D7 |
| B, H, N, T | Beta-hydroxyacyl-acp dehydratase (EC 4.2.1.-) | protein | 145 | 20% helix, 41% strand | Q965D7 |
| C, I, O, U | Beta-hydroxyacyl-acp dehydratase (EC 4.2.1.-) | protein | 144 | 22% helix, 40% strand | Q965D7 |
| D, J, P, V | Beta-hydroxyacyl-acp dehydratase (EC 4.2.1.-) | protein | 144 | 22% helix, 38% strand | Q965D7 |
| E, K, Q | Beta-hydroxyacyl-acp dehydratase (EC 4.2.1.-) | protein | 142 | 20% helix, 40% strand | Q965D7 |
| G | Beta-hydroxyacyl-acp dehydratase (EC 4.2.1.-) | protein | 147 | 21% helix, 41% strand | Q965D7 |
| W | Beta-hydroxyacyl-acp dehydratase (EC 4.2.1.-) | protein | 145 | 20% helix, 40% strand | Q965D7 |
| X | Beta-hydroxyacyl-acp dehydratase (EC 4.2.1.-) | protein | 142 | 20% helix, 37% strand | Q965D7 |
Ligands and binding sites
- K91 · 4-chloro-2-[(5-chloroquinolin-8-yl)oxy]phenol · ligand · 8 copies · chains C, D, E, F, M, N, O, P, Q, R
- PO4 · Phosphate ion · ion · chains A, B
- GOL · Glycerol · additive · 14 copies · chains A, B, D, C, E, F, G, H, I, J, K, L, M, N, P, Q, O, R, S, T, V, U, W, X
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 902 | 0.83 | 0.84 | 102 | GOL |
| 2 | 998 | 0.82 | 0.83 | 95 | GOL |
| 3 | 1015 | 0.81 | 0.82 | 93 | GOL |
| 4 | 972 | 0.80 | 0.81 | 82 | GOL |
| 5 | 1082 | 0.79 | 0.80 | 123 | empty |
Interfaces
40 interfaces between chains.
- M–N · 1430 Ų buried · 17 hydrogen bonds · protein-protein
- E–F · 1427 Ų buried · 15 hydrogen bonds · protein-protein
- Q–R · 1425 Ų buried · 14 hydrogen bonds · protein-protein
- K–L · 1421 Ų buried · 15 hydrogen bonds · protein-protein
- W–X · 1413 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 3AZ9 · Beta-Hydroxyacyl-Acyl Carrier Protein Dehydratase (FabZ) from Plasmodium falciparum in… · 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 Q965D7
- Elsewhere: RCSB PDB 3AZ9 · PDBe 3AZ9 · UniProt Q965D7
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