Research workbench
Crystal structure of human serum albumin (hsa) in complex with gn-07.
Analyse Crystal structure of human serum albumin (hsa) in complex with gn-07. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6YG9
- Type
- protein
- Length
- 568 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Serum albumin
- UniProt
- P02768
- Ligands
- MYR, OQ5
- Pockets
- 10 · best druggability 0.89
Structure
x-ray diffraction · 1 distinct chain · 68% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Serum albumin | protein | 568 | 68% helix, 0% strand | P02768 |
Ligands and binding sites
- MYR · Myristic acid · ligand · 6 copies · chains A
- OQ5 · 20-[[(2~{S})-5-[2-[2-[2-[2-[2-[2-(diethylamino)-2-oxidanylidene-ethoxy]ethoxy]ethylamino]-2-oxidanylidene-ethoxy]ethoxy]ethylamino]-1-oxidanyl-1, 5-bis(oxidanylidene)pentan-2-yl]amino]-20-oxidanylidene-icosanoic acid · ligand · 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, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1071 | 0.89 | 0.90 | 112 | MYR |
| 2 | 337 | 0.79 | 0.89 | 50 | OQ5 |
| 3 | 120 | 0.68 | 0.90 | 17 | MYR |
| 4 | 106 | 0.60 | 0.87 | 20 | MYR |
| 5 | 285 | 0.58 | 0.77 | 35 | MYR |
Modifications
Observed in the structure: 15 disulfide (disulfide).
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 6YG9 · PDBe 6YG9 · UniProt P02768
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