Research workbench
Crystal structure of human flap with an iodinated analog of mk-591
Analyse Crystal structure of human flap with an iodinated analog of mk-591 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Q7R
- Type
- protein
- Length
- 874 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Arachidonate 5-lipoxygenase-activating protein
- UniProt
- P20292
- Ligands
- 3CS
- Pockets
- 13 · best druggability 0.82
Structure
x-ray diffraction · 3 distinct chains · 71% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, E | Arachidonate 5-lipoxygenase-activating protein | protein | 140 | 76% helix, 0% strand | P20292 |
| B, D | Arachidonate 5-lipoxygenase-activating protein | protein | 148 | 68% helix, 0% strand | P20292 |
| C, F | Arachidonate 5-lipoxygenase-activating protein | protein | 149 | 70% helix, 0% strand | P20292 |
Ligands and binding sites
- 3CS · 3-[3-(3,3-dimethylbutanoyl)-1-(4-iodobenzyl)-5-(quinolin-2-ylmethoxy)-1H-indol-2-yl]-2,2-dimethylpropanoic acid · ligand · 6 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1094 | 0.82 | 0.83 | 67 | empty |
| 2 | 129 | 0.80 | 0.98 | 40 | empty |
| 3 | 1187 | 0.80 | 0.81 | 59 | empty |
| 4 | 228 | 0.70 | 0.86 | 26 | 3CS |
| 5 | 195 | 0.69 | 0.87 | 29 | 3CS |
Interfaces
7 interfaces between chains.
- A–C · 1345 Ų buried · 17 hydrogen bonds · protein-protein
- D–F · 1329 Ų buried · 17 hydrogen bonds · protein-protein
- E–F · 1262 Ų buried · 16 hydrogen bonds · protein-protein
- A–B · 1249 Ų buried · 13 hydrogen bonds · protein-protein
- B–C · 1239 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 18 modified (engineered).
Compared structures
- 2Q7R · Crystal structure of human FLAP with an iodinated analog of MK-591 · the same entry in another collection · chain F against F, TM-score 1.00
- P20292 · AlphaFold monomer V2.0 prediction for arachidonate 5-lipoxygenase- activating protein… · a predicted model of the same protein · chain A against A, TM-score 0.91
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 P20292
- Elsewhere: RCSB PDB 2Q7R · PDBe 2Q7R · UniProt P20292
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.