MolNFT v1 · #15169 · protein
Wild type myoglobin with co
1MWC · Protein (myoglobin): “Wild type myoglobin with co”. X-ray diffraction, 2 ligands (HEM, CMO), 2 pockets (best druggability 0.70). MolNFT v1 #15169 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1MWC
- Type
- protein
- Length
- 306 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (myoglobin)
- UniProt
- P02189
- Ligands
- HEM, CMO
- Pockets
- 2 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 75% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protein (myoglobin) | protein | 153 | 75% helix, 0% strand | P02189 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
- CMO · Carbon monoxide · ion · 2 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 | 197 | 0.70 | 0.87 | 29 | HEM, CMO |
| 2 | 200 | 0.70 | 0.86 | 25 | HEM, CMO |
Interfaces
1 interface between chains.
- A–B · 86 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 P02189
- Elsewhere: RCSB PDB 1MWC · PDBe 1MWC · UniProt P02189
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