Research workbench
Crystal structure of GTP binding regulator (TM1622) from thermotoga maritima at 1.75 a resolution
Analyse Crystal structure of GTP binding regulator (TM1622) from thermotoga maritima at… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1VR8
- Type
- protein
- Length
- 135 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GTP binding regulator
- UniProt
- Q9X1V7
- Ligands
- AZI
Structure
x-ray diffraction · 1 distinct chain · 21% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GTP binding regulator | protein | 135 | 21% helix, 46% strand | Q9X1V7 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 3 modified (engineered).
Compared structures
- 1VR8 · Crystal structure of GTP binding regulator (TM1622) from Thermotoga Maritima at 1.75 A… · 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 Q9X1V7
- Elsewhere: RCSB PDB 1VR8 · PDBe 1VR8 · UniProt Q9X1V7
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