Research workbench
Hsa-palmitic acid-[RUCL5(IND)]2-
Analyse Hsa-palmitic acid-[RUCL5(IND)]2- in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5GIY
- Type
- protein
- Length
- 581 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Serum albumin
- UniProt
- P02768
- Ligands
- PLM, 7GE
- Pockets
- 7 · 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 | 581 | 72% helix, 0% strand | P02768 |
Ligands and binding sites
- PLM · Palmitic acid · ligand · 6 copies · chains A
- 7GE · pentakis(chloranyl)-(1~{H}-indazol-2-ium-2-yl)ruthenium(1-) · ligand · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1007 | 0.89 | 0.91 | 106 | PLM, 7GE |
| 2 | 295 | 0.80 | 0.91 | 42 | PLM |
| 3 | 408 | 0.75 | 0.84 | 34 | PLM, 7GE |
| 4 | 262 | 0.70 | 0.84 | 32 | PLM |
| 5 | 88 | 0.60 | 0.88 | 15 | PLM |
Modifications
Observed in the structure: 17 disulfide, 5 lipid, 1 covalent (disulfide, palmitoylation, covalent ligand).
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 5GIY · PDBe 5GIY · UniProt P02768
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