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Structure of the truncated human dihydrolipoyl acetyltransferase (E2)

Analyse Structure of the truncated human dihydrolipoyl acetyltransferase (E2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3B8K
Type: protein
Length: 239 residues
Chains: 1
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dihydrolipoyllysine-residue acetyltransferase
EC: 2.3.1.12
UniProt: P10515
Pockets: 5 · best druggability 0.73

Structure

electron microscopy · 1 distinct chain · 33% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dihydrolipoyllysine-residue acetyltransferase (EC 2.3.1.12)	protein	239	33% helix, 11% strand	P10515

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	306	0.73	0.86	44	empty
2	331	0.65	0.80	42	empty
3	138	0.50	0.79	28	empty
4	119	0.41	0.76	20	empty
5	57	0.32	0.76	16	empty

Compared structures

3B8K · Structure of the Truncated Human Dihydrolipoyl Acetyltransferase (E2) · the same entry in another collection · chain A against A, TM-score 1.00
P10515 · AlphaFold monomer V2.0 prediction for dihydrolipoyllysine-residue acetyltransferase… · a predicted model of the same protein · chain A against A, TM-score 0.78

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 P10515
Elsewhere: RCSB PDB 3B8K · PDBe 3B8K · UniProt P10515

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