Research workbench
Structure of the enoyl-acp reductase fabv from yersinia pestis with the cofactor NADH and the 2-pyridone inhibitor PT172
Analyse Structure of the enoyl-acp reductase fabv from yersinia pestis with the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ZU4
- Type
- protein
- Length
- 404 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative reductase YPO4104/Y4119/YP_4011
- UniProt
- Q8Z9U1
- Ligands
- NAI, ZU4, NA
- Pockets
- 2 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative reductase YPO4104/Y4119/YP_4011 | protein | 404 | 41% helix, 18% strand | Q8Z9U1 |
Ligands and binding sites
- NAI · 1,4-dihydronicotinamide adenine dinucleotide · ligand · chains A
- ZU4 · 1-(2-chlorobenzyl)-4-hexylpyridin-2(1H)-one · ligand · chains A
- NA · Sodium ion · metal · chains A
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 | 1113 | 0.82 | 0.83 | 85 | NAI, ZU4, NA |
| 2 | 62 | 0.37 | 0.78 | 11 | empty |
Compared structures
- 3ZU4 · Structure of the enoyl-ACP reductase FabV from Yersinia pestis with the cofactor NADH and… · the same entry in another collection · chain A against A, TM-score 1.00
- Q8Z9U1 · AlphaFold monomer V2.0 prediction for enoyl-[acyl-carrier-protein] reductase [NADH]… · 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 Q8Z9U1
- Elsewhere: RCSB PDB 3ZU4 · PDBe 3ZU4 · UniProt Q8Z9U1
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