Research workbench
Crystal structure of a phospholipid-lipoxygenase complex from pseudomonas aeruginosa at 1.75A (P21212)
Analyse Crystal structure of a phospholipid-lipoxygenase complex from pseudomonas… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4G32
- Type
- protein
- Length
- 630 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 15S-lipoxygenase
- EC
- 1.13.11.-
- UniProt
- Q8RNT4
- Ligands
- ZPE, FE2
- Pockets
- 5 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 58% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 15S-lipoxygenase (EC 1.13.11.-) | protein | 630 | 58% helix, 6% strand | Q8RNT4 |
Ligands and binding sites
- ZPE · (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradec-5-enoyloxy)propyl (11Z)-octadec-11-enoate · ligand · chains A
- FE2 · Fe (II) ion · metal · chains A
- GOL · Glycerol · additive · 13 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 517 | 0.81 | 0.87 | 48 | ZPE |
| 2 | 179 | 0.64 | 0.84 | 46 | empty |
| 3 | 420 | 0.63 | 0.77 | 47 | GOL |
| 4 | 208 | 0.58 | 0.80 | 32 | empty |
| 5 | 67 | 0.29 | 0.73 | 15 | empty |
Compared structures
- 4G32 · Crystal Structure of a Phospholipid-Lipoxygenase Complex from Pseudomonas aeruginosa at… · the same entry in another collection · chain A against A, TM-score 1.00
- Q8RNT4 · AlphaFold monomer V2.0 prediction for linoleate 9/13-lipoxygenase (Q8RNT4) · 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 Q8RNT4
- Elsewhere: RCSB PDB 4G32 · PDBe 4G32 · UniProt Q8RNT4
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