Research workbench
Crystal structure of ferrous cimex nitrophorin
Analyse Crystal structure of ferrous cimex nitrophorin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2IMQ
- Type
- protein
- Length
- 280 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Salivary nitrophorin
- UniProt
- O76745
- Ligands
- HEM
- Pockets
- 2 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 16% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | Salivary nitrophorin | protein | 280 | 16% helix, 34% strand | O76745 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains X
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 271 | 0.72 | 0.86 | 35 | HEM |
| 2 | 86 | 0.34 | 0.74 | 16 | empty |
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 O76745
- Elsewhere: RCSB PDB 2IMQ · PDBe 2IMQ · UniProt O76745
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