Research workbench
Human serum albumin complexed with myristic acid and the general anesthetic halothane
Analyse Human serum albumin complexed with myristic acid and the general anesthetic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1E7C
- Type
- protein
- Length
- 582 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Serum albumin
- UniProt
- P02768
- Ligands
- HLT, MYR
- Pockets
- 10 · best druggability 0.87
Structure
x-ray diffraction · 1 distinct chain · 74% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Serum albumin | protein | 582 | 74% helix, 0% strand | P02768 |
Ligands and binding sites
- HLT · 2-bromo-2-chloro-1,1,1-trifluoroethane · ligand · 7 copies · chains A
- MYR · Myristic acid · ligand · 5 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 486 | 0.87 | 0.93 | 59 | MYR |
| 2 | 306 | 0.84 | 0.94 | 39 | MYR, HLT |
| 3 | 166 | 0.76 | 0.92 | 22 | HLT |
| 4 | 448 | 0.75 | 0.84 | 36 | MYR, HLT |
| 5 | 218 | 0.74 | 0.88 | 30 | MYR |
Modifications
Observed in the structure: 16 disulfide (disulfide).
Compared structures
- 1E7C · HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTIC ACID and the general anesthetic halothane · the same entry in another collection · chain A against A, TM-score 1.00
- P02768 · AlphaFold monomer V2.0 prediction for albumin (P02768) · a predicted model of the same protein · chain A against A, TM-score 0.84
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 P02768
- Elsewhere: RCSB PDB 1E7C · PDBe 1E7C · UniProt P02768
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