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Crystal structure of AIF2GAMMA subunit I181T from archaeon sulfolobus solfataricus complexed with gdpcp
Analyse Crystal structure of AIF2GAMMA subunit I181T from archaeon sulfolobus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6R8T
- Type
- protein
- Length
- 414 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Translation initiation factor 2 subunit gamma
- UniProt
- A0A0E3JTX3
- Ligands
- GCP, NA, MG
- Pockets
- 6 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 20% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Translation initiation factor 2 subunit gamma | protein | 414 | 20% helix, 39% strand | A0A0E3JTX3 |
Ligands and binding sites
- GCP · Phosphomethylphosphonic acid guanylate ester · ligand · chains A
- NA · Sodium ion · metal · 3 copies · chains A
- MG · Magnesium ion · metal · chains A
- FMT · Formic acid · additive · 23 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 317 | 0.60 | 0.78 | 35 | FMT, NA |
| 2 | 199 | 0.54 | 0.78 | 43 | FMT |
| 3 | 188 | 0.50 | 0.77 | 34 | FMT |
| 4 | 81 | 0.41 | 0.79 | 19 | GCP, MG |
| 5 | 56 | 0.29 | 0.75 | 16 | FMT |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 6R8T · Crystal structure of aIF2gamma subunit I181T from archaeon Sulfolobus solfataricus… · 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 A0A0E3JTX3
- Elsewhere: RCSB PDB 6R8T · PDBe 6R8T · UniProt A0A0E3JTX3
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