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Crystal structure of pyrococcus horikoshii cuta in the presence of 3M guanidine hydrochloride
Analyse Crystal structure of pyrococcus horikoshii cuta in the presence of 3M guanidine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1UMJ
- Type
- protein
- Length
- 202 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Periplasmic divalent cation tolerance protein cuta
- UniProt
- O58720
- Ligands
- GAI
- Pockets
- 1 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Periplasmic divalent cation tolerance protein cuta | protein | 101 | 37% helix, 36% strand | O58720 |
Ligands and binding sites
- GAI · Guanidine · ligand · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 95 | 0.50 | 0.82 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 204 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 1UMJ · Crystal structure of Pyrococcus horikoshii CutA in the presence of 3M guanidine… · the same entry in another collection · chain A against A, TM-score 1.00
- O58720 · AlphaFold monomer V2.0 prediction for divalent-cation tolerance protein cuta (O58720) · 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 O58720
- Elsewhere: RCSB PDB 1UMJ · PDBe 1UMJ · UniProt O58720
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