Research workbench
Crystal structure of bovine serum albumin
Analyse Crystal structure of bovine serum albumin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3V03
- Type
- protein
- Length
- 1,160 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Serum albumin
- UniProt
- P02769
- Ligands
- CA
- Pockets
- 17 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 75% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Serum albumin | protein | 581 | 75% helix, 0% strand | P02769 |
| B | Serum albumin | protein | 579 | 74% helix, 0% strand | P02769 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
17 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 951 | 0.77 | 0.80 | 65 | empty |
| 2 | 887 | 0.75 | 0.79 | 62 | empty |
| 3 | 461 | 0.73 | 0.82 | 48 | empty |
| 4 | 446 | 0.73 | 0.83 | 44 | empty |
| 5 | 121 | 0.72 | 0.92 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 184 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 34 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 P02769
- Elsewhere: RCSB PDB 3V03 · PDBe 3V03 · UniProt P02769
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