Research workbench
Crystal structure of human NADP-dependent leukotriene B4 12- hydroxydehydrogenase
Analyse Crystal structure of human NADP-dependent leukotriene B4 12… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ZSV
- Type
- protein
- Length
- 1,312 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NADP-dependent leukotriene B4 12- hydroxydehydrogenase
- UniProt
- Q14914
- Ligands
- CL
- Pockets
- 13 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | NADP-dependent leukotriene B4 12- hydroxydehydrogenase | protein | 328 | 32% helix, 26% strand | Q14914 |
Ligands and binding sites
- CL · Chloride ion · ion · 22 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 306 | 0.86 | 0.96 | 44 | empty |
| 2 | 306 | 0.86 | 0.96 | 44 | empty |
| 3 | 602 | 0.83 | 0.87 | 71 | CL |
| 4 | 561 | 0.82 | 0.88 | 64 | CL |
| 5 | 680 | 0.81 | 0.85 | 65 | CL |
Interfaces
4 interfaces between chains.
- A–B · 1171 Ų buried · 13 hydrogen bonds · protein-protein
- C–D · 1168 Ų buried · 13 hydrogen bonds · protein-protein
- A–D · 621 Ų buried · 10 hydrogen bonds · protein-protein
- B–C · 569 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 1ZSV · Crystal structure of human NADP-dependent leukotriene B4 12-hydroxydehydrogenase · the same entry in another collection · chain A against A, TM-score 1.00
- Q14914 · AlphaFold monomer V2.0 prediction for prostaglandin reductase 1 (Q14914) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q14914
- Elsewhere: RCSB PDB 1ZSV · PDBe 1ZSV · UniProt Q14914
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