Research workbench
X-ray study of human serum albumin complexed with camptothecin
Analyse X-ray study of human serum albumin complexed with camptothecin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4L9K
- Type
- protein
- Length
- 1,156 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Serum albumin
- UniProt
- P02768
- Ligands
- EHF
- Pockets
- 17 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 70% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Serum albumin | protein | 578 | 70% helix, 0% strand | P02768 |
Ligands and binding sites
- EHF · (2S)-2-hydroxy-2-[8-(hydroxymethyl)-9-oxo-9,11-dihydroindolizino[1,2-b]quinolin-7-yl]butanoic acid · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
17 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 693 | 0.82 | 0.86 | 72 | empty |
| 2 | 991 | 0.81 | 0.82 | 88 | empty |
| 3 | 549 | 0.76 | 0.83 | 46 | EHF |
| 4 | 1144 | 0.76 | 0.78 | 80 | EHF |
| 5 | 76 | 0.72 | 0.96 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 578 Ų buried · 5 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 4L9K · PDBe 4L9K · UniProt P02768
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