Research workbench
Human serum albumin complexed with myristic acid and the S-(-) enantiomer of warfarin
Analyse Human serum albumin complexed with myristic acid and the S-(-) enantiomer of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HA2
- 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, SWF
- Pockets
- 7 · best druggability 0.88
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
7 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1095 | 0.88 | 0.89 | 107 | MYR, SWF |
| 2 | 366 | 0.81 | 0.90 | 45 | MYR |
| 3 | 350 | 0.74 | 0.84 | 28 | MYR |
| 4 | 342 | 0.70 | 0.82 | 42 | MYR |
| 5 | 127 | 0.59 | 0.84 | 19 | MYR |
Modifications
Observed in the structure: 17 disulfide (disulfide).
Compared structures
- 1HA2 · Human Serum Albumin Complexed With Myristic Acid and the S-(-) enantiomer of warfarin · 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 0.85
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 1HA2 · PDBe 1HA2 · UniProt P02768
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