Research workbench
The determination of the crystal structure of recombinant pig myoglobin by molecular replacement and its refinement
Analyse The determination of the crystal structure of recombinant pig myoglobin by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1PMB
- Type
- protein
- Length
- 306 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Myoglobin
- UniProt
- P02189
- Ligands
- HEM
- Pockets
- 2 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 76% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Myoglobin | protein | 153 | 76% helix, 0% strand | P02189 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 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 | 200 | 0.71 | 0.87 | 27 | HEM |
| 2 | 200 | 0.71 | 0.87 | 26 | HEM |
Compared structures
- 1PMB · The determination of the crystal structure of recombinant pig myoglobin by molecular… · the same entry in another collection · chain A against A, TM-score 1.00
- P02189 · AlphaFold monomer V2.0 prediction for myoglobin (P02189) · 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 P02189
- Elsewhere: RCSB PDB 1PMB · PDBe 1PMB · UniProt P02189
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