Research workbench
Human serum albumin complexed with myristate and aspirin
Analyse Human serum albumin complexed with myristate and aspirin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2I2Z
- 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
- MYR, SAL
- Pockets
- 8 · best druggability 0.89
Structure
x-ray diffraction · 1 distinct chain · 72% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Serum albumin | protein | 582 | 72% helix, 0% strand | P02768 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1064 | 0.89 | 0.91 | 105 | MYR, SAL |
| 2 | 391 | 0.82 | 0.90 | 43 | MYR |
| 3 | 334 | 0.74 | 0.85 | 27 | MYR |
| 4 | 366 | 0.72 | 0.83 | 35 | MYR |
| 5 | 116 | 0.60 | 0.85 | 20 | empty |
Modifications
Observed in the structure: 17 disulfide, 1 modified (disulfide, acetylation).
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 P02768
- Elsewhere: RCSB PDB 2I2Z · PDBe 2I2Z · UniProt P02768
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