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Structure of pin-domain protein (VAPC4 toxin) from pyrococcus horikoshii determined at 1.77 a resolution
Analyse Structure of pin-domain protein (VAPC4 toxin) from pyrococcus horikoshii… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5H4G
- Type
- protein
- Length
- 284 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribonuclease VAPC4
- EC
- 3.1.-.-
- UniProt
- O58236
- Ligands
- ZN
Structure
x-ray diffraction · 2 distinct chains · 65% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonuclease VAPC4 (EC 3.1.-.-) | protein | 145 | 64% helix, 13% strand | O58236 |
| B | Ribonuclease VAPC4 (EC 3.1.-.-) | protein | 139 | 66% helix, 14% strand | O58236 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 1142 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 5H4G · Structure of PIN-domain protein (VapC4 toxin) from Pyrococcus horikoshii determined at… · the same entry in another collection · chain A against A, TM-score 1.00
- O58236 · AlphaFold monomer V2.0 prediction for ribonuclease VAPC4 (O58236) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 O58236
- Elsewhere: RCSB PDB 5H4G · PDBe 5H4G · UniProt O58236
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