Research workbench
Crystal structure of human heme oxygenase-2 in complex with myristate
Analyse Crystal structure of human heme oxygenase-2 in complex with myristate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5UC9
- Type
- protein
- Length
- 840 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heme oxygenase 2
- EC
- 1.14.14.18
- UniProt
- P30519
- Ligands
- MYR
- Pockets
- 10 · best druggability 0.84
Structure
x-ray diffraction · 3 distinct chains · 76% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Heme oxygenase 2 (EC 1.14.14.18) | protein | 209 | 76% helix, 0% strand | P30519 |
| B | Heme oxygenase 2 (EC 1.14.14.18) | protein | 211 | 75% helix, 0% strand | P30519 |
| C, D | Heme oxygenase 2 (EC 1.14.14.18) | protein | 210 | 76% helix, 0% strand | P30519 |
Ligands and binding sites
- MYR · Myristic acid · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1124 | 0.84 | 0.85 | 107 | MYR |
| 2 | 485 | 0.77 | 0.84 | 45 | MYR |
| 3 | 436 | 0.76 | 0.85 | 44 | MYR |
| 4 | 460 | 0.76 | 0.84 | 43 | MYR |
| 5 | 476 | 0.73 | 0.83 | 58 | empty |
Interfaces
5 interfaces between chains.
- A–D · 494 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 328 Ų buried · 4 hydrogen bonds · protein-protein
- B–D · 295 Ų buried · 4 hydrogen bonds · protein-protein
- A–B · 227 Ų buried · 0 hydrogen bonds · protein-protein
- C–D · 210 Ų buried · 2 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 P30519
- Elsewhere: RCSB PDB 5UC9 · PDBe 5UC9 · UniProt P30519
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.