MolNFT v1 · #126720 · protein
Binding mode of azide to ferric aplysia limacina myoglobin. crystallographic analysis at 1.9 ångströms resolution
5MBA: “Binding mode of azide to ferric aplysia limacina myoglobin. crystallographic analysis at 1.9 ångströms…”. X-ray diffraction, 3 ligands (ACE, HEM, AZI), 1 pocket (best druggability 0.73). MolNFT v1 #126720 on GenesisL1: 3D structure…
- PDB
- 5MBA
- Type
- protein
- Length
- 146 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Myoglobin
- UniProt
- P02210
- Ligands
- ACE, HEM, AZI
- Pockets
- 1 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 76% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Myoglobin | protein | 146 | 76% helix, 0% strand | P02210 |
Ligands and binding sites
- ACE · Acetyl group · ligand · chains A
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- AZI · Azide ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 239 | 0.73 | 0.87 | 29 | AZI, HEM |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 5MBA · Binding mode of azide to ferric aplysia limacina myoglobin. crystallographic analysis at… · the same entry in another collection · chain A against A, TM-score 1.00
- P02210 · AlphaFold monomer V2.0 prediction for globin (P02210) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P02210
- Elsewhere: RCSB PDB 5MBA · PDBe 5MBA · UniProt P02210
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