MolNFT v1 · #110138 · protein
X-ray structure of ALGE1
4XNK · Alginate production protein alge: “X-ray structure of ALGE1”. X-ray diffraction, 3 ligands (78M, NA, CA), 4 pockets (best druggability 0.78). MolNFT v1 #110138 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4XNK
- Type
- protein
- Length
- 421 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alginate production protein alge
- UniProt
- P18895
- Ligands
- 78M, NA, CA
- Pockets
- 4 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 1% helix, 58% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alginate production protein alge | protein | 421 | 1% helix, 58% strand | P18895 |
Ligands and binding sites
- 78M · (2S)-2,3-dihydroxypropyl(7z)-pentadec-7-enoate · ligand · chains A
- NA · Sodium ion · metal · 2 copies · chains A
- CA · Calcium ion · metal · chains A
- LDA · Lauryl dimethylamine-N-oxide · additive · 4 copies · chains A
- PE5 · 3,6,9,12,15,18,21,24-octaoxahexacosan-1-ol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 992 | 0.78 | 0.80 | 85 | empty |
| 2 | 366 | 0.69 | 0.82 | 56 | PE5 |
| 3 | 447 | 0.65 | 0.78 | 42 | empty |
| 4 | 54 | 0.36 | 0.80 | 16 | empty |
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 P18895
- Elsewhere: RCSB PDB 4XNK · PDBe 4XNK · UniProt P18895
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