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Crystal structure of BPHA3 (reduced form)
Analyse Crystal structure of BPHA3 (reduced form) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2E4Q
- Type
- protein
- Length
- 215 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Biphenyl dioxygenase ferredoxin subunit
- UniProt
- Q52440
- Ligands
- FES
- Pockets
- 2 · best druggability 0.46
Structure
x-ray diffraction · 2 distinct chains · 5% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Biphenyl dioxygenase ferredoxin subunit | protein | 108 | 3% helix, 45% strand | Q52440 |
| C | Biphenyl dioxygenase ferredoxin subunit | protein | 107 | 7% helix, 47% strand | Q52440 |
Ligands and binding sites
- FES · Fe2/s2 (inorganic) cluster · ligand · 2 copies · chains A, C
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 | 103 | 0.46 | 0.79 | 21 | empty |
| 2 | 78 | 0.31 | 0.74 | 15 | empty |
Interfaces
1 interface between chains.
- A–C · 594 Ų buried · 6 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 Q52440
- Elsewhere: RCSB PDB 2E4Q · PDBe 2E4Q · UniProt Q52440
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