Research workbench
The crystal structure of cytoglobin: the fourth globin type discovered in man
Analyse The crystal structure of cytoglobin: the fourth globin type discovered in man in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1UMO
- Type
- protein
- Length
- 308 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytoglobin
- UniProt
- Q8WWM9
- Ligands
- HEM
- Pockets
- 4 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 78% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Cytoglobin | protein | 154 | 78% helix, 0% strand | Q8WWM9 |
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
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 328 | 0.74 | 0.85 | 36 | HEM |
| 2 | 197 | 0.68 | 0.85 | 27 | HEM |
| 3 | 333 | 0.59 | 0.77 | 44 | empty |
| 4 | 245 | 0.56 | 0.78 | 33 | empty |
Interfaces
1 interface between chains.
- A–B · 762 Ų buried · 12 hydrogen bonds · protein-protein
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 Q8WWM9
- Elsewhere: RCSB PDB 1UMO · PDBe 1UMO · UniProt Q8WWM9
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