MolNFT v1 · #153503 · protein
Crystal structure of se-met cadr from P. putida with a 21 residue C- terminal truncation
6JGF: “Crystal structure of se-met cadr from P. putida with a 21 residue C- terminal truncation”. X-ray diffraction, 1 ligand (PO4), 1 pocket (best druggability 0.28). MolNFT v1 #153503 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 6JGF
- Type
- protein
- Length
- 117 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cadr
- UniProt
- Q93TP7
- Ligands
- PO4
- Pockets
- 1 · best druggability 0.28
Structure
x-ray diffraction · 1 distinct chain · 76% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cadr | protein | 117 | 76% helix, 0% strand | Q93TP7 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · chains A
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 | 64 | 0.28 | 0.72 | 13 | empty |
Modifications
Observed in the structure: 2 modified (engineered).
Compared structures
- 6JGF · Crystal structure of Se-Met CadR from P. putida with a 21 residue C-terminal truncation · 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 Q93TP7
- Elsewhere: RCSB PDB 6JGF · PDBe 6JGF · UniProt Q93TP7
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