MolNFT v1 · #31800 · protein
Structure of the dsba mutant (P31A-C33A)
2B6M · THIOL:DISULFIDE interchange protein dsba: “Structure of the dsba mutant (P31A-C33A)”. X-ray diffraction, 3 pockets (best druggability 0.77). MolNFT v1 #31800 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2B6M
- Type
- protein
- Length
- 375 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- THIOL:DISULFIDE interchange protein dsba
- UniProt
- P0AEG4
- Pockets
- 3 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 50% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | THIOL:DISULFIDE interchange protein dsba | protein | 187 | 50% helix, 11% strand | P0AEG4 |
| B | THIOL:DISULFIDE interchange protein dsba | protein | 188 | 49% helix, 11% strand | P0AEG4 |
Ligands and binding sites
- PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 487 | 0.77 | 0.85 | 56 | PEG |
| 2 | 135 | 0.46 | 0.77 | 25 | empty |
| 3 | 98 | 0.41 | 0.77 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1186 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 P0AEG4
- Elsewhere: RCSB PDB 2B6M · PDBe 2B6M · UniProt P0AEG4
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