Research workbench
Structure of human serum albumin in complex with dauda
Analyse Structure of human serum albumin in complex with dauda in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TDL
- Type
- protein
- Length
- 578 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Serum albumin
- UniProt
- P02768
- Ligands
- MYR, 11D
- Pockets
- 8 · best druggability 0.89
Structure
x-ray diffraction · 1 distinct chain · 73% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Serum albumin | protein | 578 | 73% helix, 0% strand | P02768 |
Ligands and binding sites
- MYR · Myristic acid · ligand · 4 copies · chains A
- 11D · 11-({[5-(dimethylamino)naphthalen-1-yl]sulfonyl}amino) undecanoic acid · ligand · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1168 | 0.89 | 0.90 | 119 | MYR, 11D |
| 2 | 155 | 0.75 | 0.92 | 35 | MYR |
| 3 | 137 | 0.74 | 0.92 | 26 | MYR |
| 4 | 88 | 0.59 | 0.87 | 14 | empty |
| 5 | 172 | 0.57 | 0.81 | 23 | 11D |
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 P02768
- Elsewhere: RCSB PDB 3TDL · PDBe 3TDL · UniProt P02768
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