MolNFT v1 · #29380 · protein
Structure of human ADP-ribosylation factor 4
1Z6X: “Structure of human ADP-ribosylation factor 4”. X-ray diffraction, 2 ligands (GDP, MG), 2 pockets (best druggability 0.67). MolNFT v1 #29380 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1Z6X
- Type
- protein
- Length
- 350 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ADP-ribosylation factor 4
- UniProt
- P18085
- Ligands
- GDP, MG
- Pockets
- 2 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | ADP-ribosylation factor 4 | protein | 175 | 35% helix, 29% strand | P18085 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 661 | 0.67 | 0.76 | 69 | MG, GDP |
| 2 | 50 | 0.32 | 0.77 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 603 Ų buried · 4 hydrogen bonds · protein-protein
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 P18085
- Elsewhere: RCSB PDB 1Z6X · PDBe 1Z6X · UniProt P18085
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