MolNFT v1 · #35263 · protein
Crystal structure of CUTA1 from pyrococcus horikoshii OT3, mutation D60A
2E66 · Divalent-cation tolerance protein cuta: “Crystal structure of CUTA1 from pyrococcus horikoshii OT3, mutation D60A”. X-ray diffraction, 2 ligands (NA, CL), 5 pockets (best druggability 0.85). MolNFT v1 #35263 on GenesisL1: 3D…
- PDB
- 2E66
- Type
- protein
- Length
- 306 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Divalent-cation tolerance protein cuta
- UniProt
- O58720
- Ligands
- NA, CL
- Pockets
- 5 · best druggability 0.85
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Divalent-cation tolerance protein cuta | protein | 102 | 35% helix, 39% strand | O58720 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 205 | 0.85 | 0.98 | 21 | CL |
| 2 | 107 | 0.56 | 0.84 | 17 | empty |
| 3 | 136 | 0.56 | 0.82 | 19 | empty |
| 4 | 120 | 0.54 | 0.82 | 18 | empty |
| 5 | 119 | 0.38 | 0.74 | 21 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1183 Ų buried · 20 hydrogen bonds · protein-protein
- B–C · 1165 Ų buried · 20 hydrogen bonds · protein-protein
- A–B · 1096 Ų buried · 20 hydrogen bonds · protein-protein
Compared structures
- 2E66 · Crystal Structure Of CutA1 From Pyrococcus Horikoshii OT3, Mutation D60A · 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 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 O58720
- Elsewhere: RCSB PDB 2E66 · PDBe 2E66 · UniProt O58720
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