Research workbench
Crystal structure of glorund QRRM1 domain
Analyse Crystal structure of glorund QRRM1 domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5UZG
- Type
- protein
- Length
- 174 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- AT27789P
- UniProt
- Q9VGH5
- Ligands
- SO4
Structure
x-ray diffraction · 2 distinct chains · 31% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | AT27789P | protein | 84 | 32% helix, 32% strand | Q9VGH5 |
| A | AT27789P | protein | 90 | 30% helix, 36% strand | Q9VGH5 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- B–A · 415 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 5UZG · Crystal structure of Glorund qRRM1 domain · 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 Q9VGH5
- Elsewhere: RCSB PDB 5UZG · PDBe 5UZG · UniProt Q9VGH5
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