Research workbench
Crystal structure of Y29F mutant of vitreoscilla hemoglobin
Analyse Crystal structure of Y29F mutant of vitreoscilla hemoglobin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TLD
- Type
- protein
- Length
- 288 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bacterial hemoglobin
- UniProt
- P04252
- Ligands
- HEM
- Pockets
- 4 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 83% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Bacterial hemoglobin | protein | 144 | 83% helix, 0% strand | P04252 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
- GOL · Glycerol · additive · 3 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 | 255 | 0.71 | 0.85 | 35 | HEM |
| 2 | 251 | 0.69 | 0.84 | 33 | HEM |
| 3 | 201 | 0.69 | 0.86 | 23 | empty |
| 4 | 152 | 0.54 | 0.80 | 20 | GOL |
Interfaces
1 interface between chains.
- A–B · 625 Ų buried · 2 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 P04252
- Elsewhere: RCSB PDB 3TLD · PDBe 3TLD · UniProt P04252
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