Research workbench
Structural genomics of caenorhabditis elegans: cap-gly domain of F53F4.3
Analyse Structural genomics of caenorhabditis elegans: cap-gly domain of F53F4.3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TOV
- Type
- protein
- Length
- 97 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein F53F4.3 in chromosome V
- UniProt
- Q20728
- Ligands
- SO4
Structure
x-ray diffraction · 1 distinct chain · 13% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypothetical protein F53F4.3 in chromosome V | protein | 97 | 13% helix, 32% strand | Q20728 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1TOV · Structural genomics of Caenorhabditis elegans: CAP-GLY domain of F53F4.3 · the same entry in another collection · chain A against A, TM-score 1.00
- Q20728 · AlphaFold monomer V2.0 prediction for tubulin-specific chaperone B (Q20728) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 Q20728
- Elsewhere: RCSB PDB 1TOV · PDBe 1TOV · UniProt Q20728
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