MolNFT v1 · #171203 · protein
Structure of apo-cuta
6YWP: “Structure of apo-cuta”. X-ray diffraction, 1 ligand (MG), 6 pockets (best druggability 0.70). MolNFT v1 #171203 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6YWP
- Type
- protein
- Length
- 696 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cuta
- UniProt
- G2R014
- Ligands
- MG
- Pockets
- 6 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cuta | protein | 350 | 47% helix, 14% strand | G2R014 |
| B | Cuta | protein | 346 | 48% helix, 11% strand | G2R014 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 785 | 0.70 | 0.76 | 69 | empty |
| 2 | 704 | 0.68 | 0.76 | 52 | empty |
| 3 | 123 | 0.42 | 0.76 | 23 | empty |
| 4 | 82 | 0.34 | 0.76 | 23 | empty |
| 5 | 64 | 0.29 | 0.74 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 795 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 6YWP · Structure of apo-CutA · the same entry in another collection · 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 G2R014
- Elsewhere: RCSB PDB 6YWP · PDBe 6YWP · UniProt G2R014
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