Research workbench
Engineered human lipocalin 2 with specificity for Y-dtpa, apo-form
Analyse Engineered human lipocalin 2 with specificity for Y-dtpa, apo-form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3DTQ
- Type
- protein
- Length
- 511 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Neutrophil gelatinase-associated lipocalin
- UniProt
- P80188
- Pockets
- 5 · best druggability 0.64
Structure
x-ray diffraction · 3 distinct chains · 12% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Neutrophil gelatinase-associated lipocalin | protein | 171 | 12% helix, 44% strand | P80188 |
| B | Neutrophil gelatinase-associated lipocalin | protein | 168 | 11% helix, 45% strand | P80188 |
| C | Neutrophil gelatinase-associated lipocalin | protein | 172 | 13% helix, 44% strand | P80188 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 415 | 0.64 | 0.78 | 39 | empty |
| 2 | 372 | 0.61 | 0.77 | 44 | empty |
| 3 | 291 | 0.58 | 0.77 | 37 | empty |
| 4 | 107 | 0.38 | 0.74 | 17 | empty |
| 5 | 118 | 0.37 | 0.74 | 26 | empty |
Interfaces
2 interfaces between chains.
- A–C · 434 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 197 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 3DTQ · Engineered human lipocalin 2 with specificity for Y-DTPA, apo-form · 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 P80188
- Elsewhere: RCSB PDB 3DTQ · PDBe 3DTQ · UniProt P80188
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