MolNFT v1 · #150820 · protein

Core of the human pyruvate dehydrogenase (E2)

6H55 · Dihydrolipoyllysine-residue acetyltransferase component of…: “Core of the human pyruvate dehydrogenase (E2)”. Electron microscopy, 1 pocket (best druggability 0.67). MolNFT v1 #150820 on GenesisL1: 3D structure, binding sites and…

PDB: 6H55
Type: protein
Length: 233 residues
Chains: 1
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase…
EC: 2.3.1.12
UniProt: P10515
Pockets: 1 · best druggability 0.67

Structure

electron microscopy · 1 distinct chain · 37% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial (EC 2.3.1.12)	protein	233	37% helix, 19% strand	P10515

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1187	0.67	0.74	121	empty

Compared structures

6H55 · core of the human pyruvate dehydrogenase (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 0.95

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 6H55 · PDBe 6H55 · UniProt P10515

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