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The structure of HMG/CHA aldolase from the protocatechuate degradation pathway of pseudomonas putida

Analyse The structure of HMG/CHA aldolase from the protocatechuate degradation pathway… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3NOJ
Type: protein
Length: 235 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 4-carboxy-4-hydroxy-2-oxoadipate ALDOLASE/OXALOACETATE decarboxylase
EC: 4.1.3.17
UniProt: A5W059
Ligands: PYR, MG

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	4-carboxy-4-hydroxy-2-oxoadipate ALDOLASE/OXALOACETATE decarboxylase (EC 4.1.3.17)	protein	235	34% helix, 25% strand	A5W059

Ligands and binding sites

PYR · Pyruvic acid · ligand · chains A
MG · Magnesium ion · metal · chains A
PG4 · Tetraethylene glycol · additive · 2 copies · chains A

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

Compared structures

3NOJ · The structure of HMG/CHA aldolase from the protocatechuate degradation pathway of… · the same entry in another collection · chain A against A, TM-score 1.00
A5W059 · AlphaFold monomer V2.0 prediction for 4-hydroxy-4-methyl-2-oxoglutarate… · a predicted model of the same protein · chain A against A, TM-score 0.99

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Every structure of UniProt A5W059
Elsewhere: RCSB PDB 3NOJ · PDBe 3NOJ · UniProt A5W059

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