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Crystallographic and enzymatic investigations on the role of SER558, HIS610 and ASN614 in the catalytic mechanism of azotobacter vinelandii dihydrolipoamide acetyltransferase (E2P)

Analyse Crystallographic and enzymatic investigations on the role of SER558, HIS610 and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1DPB
Type: protein
Length: 243 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dihydrolipoyl-transacetylase
EC: 2.3.1.12
UniProt: P10802
Pockets: 2 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dihydrolipoyl-transacetylase (EC 2.3.1.12)	protein	243	40% helix, 23% strand	P10802

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	296	0.56	0.76	38	empty
2	197	0.50	0.76	31	empty

Compared structures

1DPB · Crystallographic and enzymatic investigations on the role of SER558, HIS610 and ASN614 in… · the same entry in another collection · chain A against A, TM-score 1.00
P10802 · AlphaFold monomer V2.0 prediction for dihydrolipoyllysine-residue acetyltransferase… · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P10802
Elsewhere: RCSB PDB 1DPB · PDBe 1DPB · UniProt P10802

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