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Structure of an ADP ribosylation factor from entamoeba histolytica hm- 1:IMSS bound to mg-GDP
Analyse Structure of an ADP ribosylation factor from entamoeba histolytica hm- 1:IMSS… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4YLG
- Type
- protein
- Length
- 326 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ADP-ribosylation factor
- UniProt
- C4LXL1
- Ligands
- GDP, MG
- Pockets
- 1 · best druggability 0.63
Structure
x-ray diffraction · 2 distinct chains · 32% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ADP-ribosylation factor | protein | 165 | 34% helix, 32% strand | C4LXL1 |
| B | ADP-ribosylation factor | protein | 161 | 30% helix, 31% strand | C4LXL1 |
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
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 | 468 | 0.63 | 0.76 | 55 | GDP, MG |
Interfaces
1 interface between chains.
- A–B · 619 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 4YLG · Structure of an ADP ribosylation factor from Entamoeba histolytica HM-1:IMSS bound to… · the same entry in another collection · chain A against A, TM-score 1.00
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 C4LXL1
- Elsewhere: RCSB PDB 4YLG · PDBe 4YLG · UniProt C4LXL1
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