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Crystal structure of equine serum albumin
Analyse Crystal structure of equine serum albumin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4F5T
- Type
- protein
- Length
- 583 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Serum albumin
- UniProt
- P35747
- Ligands
- SO4
- Pockets
- 12 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 73% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Serum albumin | protein | 583 | 73% helix, 0% strand | P35747 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains A
- GOL · Glycerol · additive · 8 copies · chains A
- ACT · Acetate ion · additive · 6 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 591 | 0.80 | 0.86 | 67 | ACT, SO4 |
| 2 | 214 | 0.78 | 0.91 | 29 | ACT, GOL |
| 3 | 69 | 0.73 | 0.97 | 19 | ACT |
| 4 | 620 | 0.73 | 0.80 | 51 | GOL |
| 5 | 219 | 0.62 | 0.82 | 23 | ACT |
Modifications
Observed in the structure: 17 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 P35747
- Elsewhere: RCSB PDB 4F5T · PDBe 4F5T · UniProt P35747
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