Research workbench
Crystal structure of human biliverdin reductase a
Analyse Crystal structure of human biliverdin reductase a in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2H63
- Type
- protein
- Length
- 1,131 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Biliverdin reductase a
- EC
- 1.3.1.24
- UniProt
- P53004
- Ligands
- NAP
- Pockets
- 11 · best druggability 0.78
Structure
x-ray diffraction · 4 distinct chains · 41% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Biliverdin reductase a (EC 1.3.1.24) | protein | 284 | 41% helix, 27% strand | P53004 |
| B | Biliverdin reductase a (EC 1.3.1.24) | protein | 279 | 42% helix, 27% strand | P53004 |
| C | Biliverdin reductase a (EC 1.3.1.24) | protein | 283 | 41% helix, 27% strand | P53004 |
| D | Biliverdin reductase a (EC 1.3.1.24) | protein | 285 | 41% helix, 26% strand | P53004 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 4 copies · chains A, D, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 886 | 0.78 | 0.80 | 86 | NAP |
| 2 | 911 | 0.71 | 0.76 | 65 | empty |
| 3 | 971 | 0.71 | 0.75 | 70 | empty |
| 4 | 504 | 0.66 | 0.77 | 51 | NAP |
| 5 | 387 | 0.59 | 0.76 | 42 | NAP |
Interfaces
4 interfaces between chains.
- A–C · 999 Ų buried · 7 hydrogen bonds · protein-protein
- B–D · 930 Ų buried · 4 hydrogen bonds · protein-protein
- A–B · 310 Ų buried · 3 hydrogen bonds · protein-protein
- A–D · 119 Ų buried · 1 hydrogen bond · 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 P53004
- Elsewhere: RCSB PDB 2H63 · PDBe 2H63 · UniProt P53004
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