MolNFT v1 · #122212 · protein
Crystal structure of equine serum albumin in the presence of 2.5 mm zinc at pH 7.4
5IIH: “Crystal structure of equine serum albumin in the presence of 2.5 mm zinc at pH 7.4”. X-ray diffraction, 2 ligands (ZN, SO4), 7 pockets (best druggability 0.81). MolNFT v1 #122212 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 5IIH
- Type
- protein
- Length
- 580 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Serum albumin
- UniProt
- P35747
- Ligands
- ZN, SO4
- Pockets
- 7 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 75% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Serum albumin | protein | 580 | 75% helix, 0% strand | P35747 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 565 | 0.81 | 0.86 | 58 | SO4 |
| 2 | 874 | 0.79 | 0.82 | 64 | empty |
| 3 | 246 | 0.65 | 0.82 | 41 | empty |
| 4 | 220 | 0.58 | 0.79 | 27 | empty |
| 5 | 215 | 0.50 | 0.75 | 28 | empty |
Modifications
Observed in the structure: 17 disulfide (disulfide).
Compared structures
- 5IIH · Crystal structure of Equine Serum Albumin in the presence of 2.5 mM zinc at pH 7.4 · the same entry in another collection · chain A against A, TM-score 1.00
- P35747 · AlphaFold monomer V2.0 prediction for albumin (P35747) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P35747
- Elsewhere: RCSB PDB 5IIH · PDBe 5IIH · UniProt P35747
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