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Crystal structure of human biliverdin IX-beta reductase B
Analyse Crystal structure of human biliverdin IX-beta reductase B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7ER6
- Type
- protein
- Length
- 412 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flavin reductase (NADPH)
- EC
- 1.5.1.30, 1.3.1.24
- UniProt
- P30043
- Ligands
- NAP, SO4
- Pockets
- 2 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Flavin reductase (NADPH) (EC 1.5.1.30, 1.3.1.24) | protein | 206 | 36% helix, 21% strand | P30043 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 928 | 0.82 | 0.84 | 80 | SO4, NAP |
| 2 | 509 | 0.73 | 0.82 | 50 | NAP |
Interfaces
1 interface between chains.
- A–B · 629 Ų buried · 7 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 P30043
- Elsewhere: RCSB PDB 7ER6 · PDBe 7ER6 · UniProt P30043
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