Research workbench
Crystal structure of E.COLI CUTA1 C16A/C39A/C79A mutation
Analyse Crystal structure of E.COLI CUTA1 C16A/C39A/C79A mutation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4Y65
- Type
- protein
- Length
- 325 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Divalent-cation tolerance protein cuta
- UniProt
- P69488
- Pockets
- 4 · best druggability 0.76
Structure
x-ray diffraction · 3 distinct chains · 34% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Divalent-cation tolerance protein cuta | protein | 112 | 32% helix, 39% strand | P69488 |
| B | Divalent-cation tolerance protein cuta | protein | 109 | 34% helix, 40% strand | P69488 |
| C | Divalent-cation tolerance protein cuta | protein | 104 | 35% helix, 42% strand | P69488 |
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 68 | 0.76 | 0.98 | 18 | empty |
| 2 | 102 | 0.60 | 0.87 | 19 | empty |
| 3 | 91 | 0.54 | 0.84 | 17 | empty |
| 4 | 135 | 0.54 | 0.81 | 17 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1209 Ų buried · 15 hydrogen bonds · protein-protein
- A–B · 1199 Ų buried · 15 hydrogen bonds · protein-protein
- B–C · 1089 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 4Y65 · Crystal structure of E.coli CutA1 C16A/C39A/C79A mutation · the same entry in another collection · chain C against C, TM-score 1.00
- P69488 · AlphaFold monomer V2.0 prediction for divalent-cation tolerance protein cuta (P69488) · a predicted model of the same protein · chain C against A, TM-score 0.98
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 P69488
- Elsewhere: RCSB PDB 4Y65 · PDBe 4Y65 · UniProt P69488
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