MolNFT v1 · #92777 · protein
Crystal structure of human gltp bound with 12:0 disulfatide
4GIX · Glycolipid transfer protein: “Crystal structure of human gltp bound with 12:0 disulfatide”. X-ray diffraction, 1 ligand (0SG), 1 pocket (best druggability 0.68). MolNFT v1 #92777 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 4GIX
- Type
- protein
- Length
- 207 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycolipid transfer protein
- UniProt
- Q9NZD2
- Ligands
- 0SG
- Pockets
- 1 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 66% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycolipid transfer protein | protein | 207 | 66% helix, 1% strand | Q9NZD2 |
Ligands and binding sites
- 0SG · N-{(2S,3R,4E)-1-[(3,6-di-O-sulfo-beta-D-galactopyranosyl)oxy]-3-hydroxyoctadec-4-en-2-yl}dodecanamide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 240 | 0.68 | 0.84 | 30 | 0SG |
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 Q9NZD2
- Elsewhere: RCSB PDB 4GIX · PDBe 4GIX · UniProt Q9NZD2
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