MolNFT v1 · #32901 · protein

Structure of aminoadipate-semialdehyde dehydrogenase- phosphopantetheinyl transferase in complex with coenzyme a

2C43 · Aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl…: “Structure of aminoadipate-semialdehyde dehydrogenase- phosphopantetheinyl transferase in complex with…”. X-ray diffraction, 3 ligands (COA, MG, CL), 2 pockets (best…

PDB: 2C43
Type: protein
Length: 280 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase
EC: 1.2.1.31
UniProt: Q9P0Q3
Ligands: COA, MG, CL
Pockets: 2 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase (EC 1.2.1.31)	protein	280	34% helix, 24% strand	Q9P0Q3

Ligands and binding sites

COA · Coenzyme A · ligand · chains A
MG · Magnesium ion · metal · chains A
CL · Chloride ion · ion · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 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	238	0.55	0.77	34	COA, MG
2	146	0.47	0.77	26	empty

Compared structures

2C43 · Structure of aminoadipate-semialdehyde dehydrogenase- phosphopantetheinyl transferase in… · the same entry in another collection · chain A against A, TM-score 1.00

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 Q9P0Q3
Elsewhere: RCSB PDB 2C43 · PDBe 2C43 · UniProt Q9P0Q3

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