MolNFT v1 · #4480 · protein

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

1DPD · Dihydrolipoyl-transacetylase: “Crystallographic and enzymatic investigations on the role of SER558, HIS610 and ASN614 in the catalytic…”. X-ray diffraction, 3 pockets (best druggability 0.53). MolNFT v1 #4480 on GenesisL1: 3D…

PDB: 1DPD
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: 3 · best druggability 0.53

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

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	255	0.53	0.76	33	empty
2	199	0.50	0.76	31	empty
3	60	0.33	0.76	14	empty

Compared structures

1DPD · 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 1DPD · PDBe 1DPD · UniProt P10802

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