Research workbench
Crystal structure of leishmania major ADP ribosylation factor-like 1.
Analyse Crystal structure of leishmania major ADP ribosylation factor-like 1. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2X77
- Type
- protein
- Length
- 347 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ADP-ribosylation factor
- UniProt
- Q4QEJ1
- Ligands
- GDP, MG
- Pockets
- 1 · best druggability 0.53
Structure
x-ray diffraction · 2 distinct chains · 29% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ADP-ribosylation factor | protein | 181 | 27% helix, 24% strand | Q4QEJ1 |
| B | ADP-ribosylation factor | protein | 166 | 31% helix, 25% strand | Q4QEJ1 |
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 | 280 | 0.53 | 0.75 | 32 | empty |
Interfaces
1 interface between chains.
- A–B · 232 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 2X77 · Crystal Structure of Leishmania major ADP ribosylation factor-like 1. · the same entry in another collection · chain B against B, 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 Q4QEJ1
- Elsewhere: RCSB PDB 2X77 · PDBe 2X77 · UniProt Q4QEJ1
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