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Crystal structure of THR134 to ala of ST1022-glutamine complex from sulfolobus tokodaii 7
Analyse Crystal structure of THR134 to ala of ST1022-glutamine complex from sulfolobus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2EFQ
- Type
- protein
- Length
- 150 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 150AA long hypothetical transcriptional regulator
- UniProt
- Q972W6
- Ligands
- GLN, MG
- Pockets
- 1 · best druggability 0.46
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 150AA long hypothetical transcriptional regulator | protein | 150 | 38% helix, 20% strand | Q972W6 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 180 | 0.46 | 0.75 | 19 | MG |
Compared structures
- 2EFQ · Crystal Structure of Thr134 to Ala of ST1022-Glutamine Complex from Sulfolobus tokodaii 7 · 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 Q972W6
- Elsewhere: RCSB PDB 2EFQ · PDBe 2EFQ · UniProt Q972W6
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