Research workbench
PHE46(CD4) orients the distal histidine for hydrogen bonding to bound ligands in sperm whale myoglobin
Analyse PHE46(CD4) orients the distal histidine for hydrogen bonding to bound ligands… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MTI
- Type
- protein
- Length
- 154 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Myoglobin
- UniProt
- P02185
- Ligands
- HEM, SO4
- Pockets
- 1 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 78% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Myoglobin | protein | 154 | 78% helix, 0% strand | P02185 |
Ligands and binding sites
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 | 220 | 0.71 | 0.86 | 26 | HEM |
Compared structures
- 1MTI · PHE46(CD4) orients the distal histidine for hydrogen bonding to bound ligands in sperm… · the same entry in another collection · chain A against A, TM-score 1.00
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 P02185
- Elsewhere: RCSB PDB 1MTI · PDBe 1MTI · UniProt P02185
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