MolNFT v1 · #15631 · protein
Crystal structure of CUTA1 from E.COLI at 1.7 a resolution
1NAQ · Periplasmic divalent cation tolerance protein cuta: “Crystal structure of CUTA1 from E.COLI at 1.7 a resolution”. X-ray diffraction, 2 ligands (MBO, HG), 14 pockets (best druggability 0.79). MolNFT v1 #15631 on GenesisL1: 3D…
- PDB
- 1NAQ
- Type
- protein
- Length
- 628 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Periplasmic divalent cation tolerance protein cuta
- UniProt
- P69488
- Ligands
- MBO, HG
- Pockets
- 14 · best druggability 0.79
Structure
x-ray diffraction · 5 distinct chains · 35% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Periplasmic divalent cation tolerance protein cuta | protein | 106 | 35% helix, 41% strand | P69488 |
| B | Periplasmic divalent cation tolerance protein cuta | protein | 103 | 35% helix, 42% strand | P69488 |
| C, F | Periplasmic divalent cation tolerance protein cuta | protein | 105 | 35% helix, 42% strand | P69488 |
| D | Periplasmic divalent cation tolerance protein cuta | protein | 104 | 35% helix, 41% strand | P69488 |
| E | Periplasmic divalent cation tolerance protein cuta | protein | 105 | 34% helix, 41% strand | P69488 |
Ligands and binding sites
- MBO · Mercuribenzoic acid · ligand · 10 copies · chains A, C, B, D, E, F
- HG · Mercury (II) ion · metal · 8 copies · chains A, B, C, D, F, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 104 | 0.79 | 0.97 | 18 | empty |
| 2 | 86 | 0.77 | 0.97 | 18 | empty |
| 3 | 196 | 0.68 | 0.87 | 24 | empty |
| 4 | 162 | 0.66 | 0.87 | 21 | empty |
| 5 | 261 | 0.61 | 0.79 | 26 | HG, MBO |
Interfaces
12 interfaces between chains.
- A–C · 1106 Ų buried · 14 hydrogen bonds · protein-protein
- B–C · 1073 Ų buried · 14 hydrogen bonds · protein-protein
- D–E · 1073 Ų buried · 15 hydrogen bonds · protein-protein
- D–F · 1071 Ų buried · 16 hydrogen bonds · protein-protein
- A–B · 1065 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 1NAQ · Crystal structure of CUTA1 from E.coli at 1.7 A resolution · the same entry in another collection · chain F against F, 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 0.95
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 1NAQ · PDBe 1NAQ · UniProt P69488
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