MolNFT v1 · #27700 · protein
Crystal structure of a mutant bleomycin binding protein from streptoalloteichus hindustanus displaying increased thermostability
1XRK · Bleomycin resistance protein: “Crystal structure of a mutant bleomycin binding protein from streptoalloteichus hindustanus displaying…”. X-ray diffraction, 2 ligands (BLM, SO4), 2 pockets (best druggability 0.35). MolNFT v1 #27700…
- PDB
- 1XRK
- Type
- protein
- Length
- 241 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bleomycin resistance protein
- UniProt
- P17493
- Ligands
- BLM, SO4
- Pockets
- 2 · best druggability 0.35
Structure
x-ray diffraction · 2 distinct chains · 19% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bleomycin resistance protein | protein | 120 | 18% helix, 46% strand | P17493 |
| B | Bleomycin resistance protein | protein | 121 | 19% helix, 45% strand | P17493 |
Ligands and binding sites
- BLM · Bleomycin A2 · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 57 | 0.35 | 0.77 | 11 | empty |
| 2 | 51 | 0.30 | 0.75 | 11 | empty |
Interfaces
1 interface between chains.
- A–B · 1685 Ų buried · 26 hydrogen bonds · protein-protein
Compared structures
- 1XRK · Crystal structure of a mutant bleomycin binding protein from Streptoalloteichus… · the same entry in another collection · chain A against A, TM-score 1.00
- P17493 · AlphaFold monomer V2.0 prediction for bleomycin resistance protein (P17493) · a predicted model of the same protein · chain B 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 P17493
- Elsewhere: RCSB PDB 1XRK · PDBe 1XRK · UniProt P17493
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