Research workbench
Cobra ngf in complex with lipid
Analyse Cobra ngf in complex with lipid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4EC7
- Type
- protein
- Length
- 216 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Venom nerve growth factor
- UniProt
- P61898
- Ligands
- L44
- Pockets
- 3 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 65% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Venom nerve growth factor | protein | 108 | 0% helix, 65% strand | P61898 |
Ligands and binding sites
- L44 · (2S)-1-hydroxy-3-(tetradecanoyloxy)propan-2-yl docosanoate · ligand · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 254 | 0.72 | 0.86 | 31 | L44 |
| 2 | 57 | 0.29 | 0.75 | 13 | empty |
| 3 | 50 | 0.29 | 0.76 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1429 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
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 P61898
- Elsewhere: RCSB PDB 4EC7 · PDBe 4EC7 · UniProt P61898
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