Research workbench
Crystal structure of the heme pas sensor domain of ec dos (ferrous form)
Analyse Crystal structure of the heme pas sensor domain of ec dos (ferrous form) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1V9Z
- Type
- protein
- Length
- 226 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heme pas sensor protein
- Ligands
- HEM
- Pockets
- 3 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Heme pas sensor protein | protein | 113 | 26% helix, 34% strand | — |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · 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, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 254 | 0.72 | 0.86 | 29 | HEM |
| 2 | 248 | 0.69 | 0.84 | 30 | HEM |
| 3 | 278 | 0.57 | 0.77 | 42 | empty |
Interfaces
1 interface between chains.
- A–B · 1210 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 1V9Z · Crystal Structure of the heme PAS sensor domain of Ec DOS (Ferrous 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
- Elsewhere: RCSB PDB 1V9Z · PDBe 1V9Z
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