Research workbench
D136A mutant of heme oxygenase from corynebacterium diphtheriae (hmuo)
Analyse D136A mutant of heme oxygenase from corynebacterium diphtheriae (hmuo) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1WNV
- Type
- protein
- Length
- 624 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heme oxygenase
- EC
- 1.14.99.3
- UniProt
- P71119
- Ligands
- HEM, SO4
- Pockets
- 4 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 78% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Heme oxygenase (EC 1.14.99.3) | protein | 207 | 79% helix, 0% strand | P71119 |
| B | Heme oxygenase (EC 1.14.99.3) | protein | 210 | 77% helix, 0% strand | P71119 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 3 copies · chains A, B, C
- SO4 · Sulfate ion · ion · 5 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 357 | 0.73 | 0.84 | 34 | HEM |
| 2 | 373 | 0.73 | 0.84 | 33 | HEM |
| 3 | 336 | 0.72 | 0.84 | 34 | HEM |
| 4 | 637 | 0.69 | 0.78 | 71 | SO4 |
Interfaces
3 interfaces between chains.
- B–C · 698 Ų buried · 16 hydrogen bonds · protein-protein
- A–B · 625 Ų buried · 7 hydrogen bonds · protein-protein
- A–C · 10 Ų buried · 0 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 P71119
- Elsewhere: RCSB PDB 1WNV · PDBe 1WNV · UniProt P71119
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