Research workbench
Heme-ligand tunneling in group I truncated hemoglobins
Analyse Heme-ligand tunneling in group I truncated hemoglobins in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1UVY
- Type
- protein
- Length
- 116 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Myoglobin
- UniProt
- P15160
- Ligands
- HEM, XE
- Pockets
- 1 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 69% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Myoglobin | protein | 116 | 69% helix, 0% strand | P15160 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 296 | 0.75 | 0.87 | 31 | HEM |
Compared structures
- 1UVY · Heme-ligand tunneling in group I truncated hemoglobins · the same entry in another collection · chain A against A, TM-score 1.00
- P15160 · AlphaFold monomer V2.0 prediction for group 1 truncated hemoglobin trhbn (P15160) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P15160
- Elsewhere: RCSB PDB 1UVY · PDBe 1UVY · UniProt P15160
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.