Research workbench
Crystal structure of LTBP1 LTC4 complex collected on an in-house source
Analyse Crystal structure of LTBP1 LTC4 complex collected on an in-house source in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5HAE
- Type
- protein
- Length
- 155 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lipocalin ai-4
- UniProt
- Q7YT09
- Ligands
- EAH, GSH
- Pockets
- 1 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 8% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lipocalin ai-4 | protein | 155 | 8% helix, 42% strand | Q7YT09 |
Ligands and binding sites
- EAH · (5S,7E,9E,11Z,14Z)-5-hydroxyicosa-7,9,11,14-tetraenoic acid · ligand · chains A
- GSH · Glutathione · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 337 | 0.74 | 0.85 | 41 | EAH, GSH |
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 5HAE · Crystal structure of LTBP1 LTC4 complex collected on an in-house source · 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 Q7YT09
- Elsewhere: RCSB PDB 5HAE · PDBe 5HAE · UniProt Q7YT09
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