Research workbench
NMR structure of hmg-acpi domain from cura module from lyngbya majuscula
Analyse NMR structure of hmg-acpi domain from cura module from lyngbya majuscula in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2LIW
- Type
- protein
- Length
- 99 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cura
- UniProt
- Q6DNF2
- Ligands
- PNS, MAH
- Pockets
- 1 · best druggability 0.38
Structure
solution nmr · 1 distinct chain · 56% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cura | protein | 99 | 56% helix, 0% strand | Q6DNF2 |
Ligands and binding sites
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 | 53 | 0.38 | 0.81 | 17 | empty |
Modifications
Observed in the structure: 1 cofactor (phosphopantetheinylation).
Compared structures
- 2LIW · NMR structure of HMG-ACPI domain from CurA module from Lyngbya majuscula · 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 Q6DNF2
- Elsewhere: RCSB PDB 2LIW · PDBe 2LIW · UniProt Q6DNF2
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