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Crystal structure of the catalytic domain of at-higle
Analyse Crystal structure of the catalytic domain of at-higle in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7WME
- Type
- protein
- Length
- 153 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Structure-specific endonuclease subunit SLX1 homolog
- EC
- 3.1.-.-
- UniProt
- Q682H4
- Ligands
- CA
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Structure-specific endonuclease subunit SLX1 homolog (EC 3.1.-.-) | protein | 153 | 39% helix, 19% strand | Q682H4 |
Ligands and binding sites
- CA · Calcium ion · metal
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7WME · Crystal Structure of the catalytic domain of At-HIGLE · 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 Q682H4
- Elsewhere: RCSB PDB 7WME · PDBe 7WME · UniProt Q682H4
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