Research workbench
Structure of a triple mutant of asv-tftrhb
Analyse Structure of a triple mutant of asv-tftrhb in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4UZV
- Type
- protein
- Length
- 129 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hemoglobin
- UniProt
- R9F4S3
- Ligands
- HEM
- Pockets
- 2 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 62% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hemoglobin | protein | 129 | 62% helix, 0% strand | R9F4S3 |
Ligands and binding sites
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 | 460 | 0.79 | 0.86 | 35 | HEM, ACT |
| 2 | 55 | 0.30 | 0.75 | 13 | empty |
Compared structures
- 4UZV · Structure of a triple mutant of ASV-TfTrHb · 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
- Every structure of UniProt R9F4S3
- Elsewhere: RCSB PDB 4UZV · PDBe 4UZV · UniProt R9F4S3
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