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Solution NMR structure of putative N-acetyl transferase yhhk from E. COLI bound to coenzyme a: northeast structural genomics consortium target ET106

Analyse Solution NMR structure of putative N-acetyl transferase yhhk from E. COLI bound… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2K5T
Type: protein
Length: 128 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized protein yhhk
UniProt: P37613
Ligands: COA
Pockets: 3 · best druggability 0.58

Structure

solution nmr · 1 distinct chain · 26% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uncharacterized protein yhhk	protein	128	26% helix, 33% strand	P37613

Ligands and binding sites

COA · Coenzyme A · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	222	0.58	0.80	31	COA
2	52	0.33	0.78	12	empty
3	52	0.33	0.77	14	empty

Compared structures

2K5T · Solution NMR Structure of Putative N-Acetyl Transferase YhhK from E. coli Bound to… · the same entry in another collection · chain A against A, TM-score 1.00
P37613 · AlphaFold monomer V2.0 prediction for pand regulatory factor (P37613) · a predicted model of the same protein · chain A against A, TM-score 0.89

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 P37613
Elsewhere: RCSB PDB 2K5T · PDBe 2K5T · UniProt P37613

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