Research workbench
Hsa ligand free
Analyse Hsa ligand free in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4K2C
- Type
- protein
- Length
- 1,158 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Serum albumin
- UniProt
- P02768
- Pockets
- 20 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 71% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Serum albumin | protein | 579 | 71% helix, 0% strand | P02768 |
Pockets
20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 959 | 0.86 | 0.87 | 100 | empty |
| 2 | 449 | 0.82 | 0.89 | 47 | empty |
| 3 | 536 | 0.78 | 0.85 | 54 | empty |
| 4 | 138 | 0.69 | 0.89 | 23 | empty |
| 5 | 127 | 0.69 | 0.90 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 592 Ų buried · 3 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 P02768
- Elsewhere: RCSB PDB 4K2C · PDBe 4K2C · UniProt P02768
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