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Dihydrolipoyl transacetylase (E.C.2.3.1.12) catalytic domain (residues 184-425) from bacillus stearothermophilus

Analyse Dihydrolipoyl transacetylase (E.C.2.3.1.12) catalytic domain (residues 184-425)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1B5S
Type: protein
Length: 1,210 residues
Chains: 5
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dihydrolipoamide acetyltransferase
EC: 2.3.1.12
UniProt: P11961
Pockets: 16 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E	Dihydrolipoamide acetyltransferase (EC 2.3.1.12)	protein	242	36% helix, 19% strand	P11961

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	960	0.78	0.80	102	empty
2	902	0.78	0.81	105	empty
3	895	0.77	0.81	104	empty
4	964	0.77	0.80	108	empty
5	973	0.77	0.80	105	empty

Compared structures

1B5S · Dihydrolipoyl transacetylase (E.C.2.3.1.12) catalytic domain (residues 184-425) from… · the same entry in another collection · chain A against A, TM-score 1.00
P11961 · AlphaFold monomer V2.0 prediction for dihydrolipoyllysine-residue acetyltransferase… · a predicted model of the same protein · chain A against A, TM-score 0.94

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 P11961
Elsewhere: RCSB PDB 1B5S · PDBe 1B5S · UniProt P11961

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