Research workbench
X-ray study of human serum albumin complexed with heme
Analyse X-ray study of human serum albumin complexed with heme in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1N5U
- Type
- protein
- Length
- 583 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Serum albumin
- UniProt
- P02768
- Ligands
- MYR, HEM
- Pockets
- 8 · best druggability 0.88
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 | P02768 |
Ligands and binding sites
- MYR · Myristic acid · ligand · 5 copies · chains A
- HEM · Protoporphyrin IX containing Fe · ligand · 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 | 1113 | 0.88 | 0.88 | 112 | MYR |
| 2 | 293 | 0.79 | 0.90 | 41 | MYR |
| 3 | 367 | 0.76 | 0.86 | 31 | HEM |
| 4 | 214 | 0.69 | 0.86 | 29 | MYR |
| 5 | 99 | 0.58 | 0.86 | 19 | MYR |
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 1N5U · PDBe 1N5U · UniProt P02768
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