MolNFT v1 · #116069 · protein

4-oxalocrotonate decarboxylase from pseudomonas putida G7 - complexed with magnesium

5D2G · 4-oxalocrotonate decarboxylase nahk: “4-oxalocrotonate decarboxylase from pseudomonas putida G7 - complexed with magnesium”. X-ray diffraction, 3 ligands (MG, CL, SO4), 2 pockets (best druggability 0.63). MolNFT v1 #116069 on…

PDB: 5D2G
Type: protein
Length: 263 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 4-oxalocrotonate decarboxylase nahk
EC: 4.1.1.77
UniProt: Q1XGK3
Ligands: MG, CL, SO4
Pockets: 2 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	4-oxalocrotonate decarboxylase nahk (EC 4.1.1.77)	protein	263	32% helix, 30% strand	Q1XGK3

Ligands and binding sites

MG · Magnesium ion · metal · chains A
CL · Chloride ion · ion · 2 copies · chains A
SO4 · Sulfate ion · ion · chains A
EDO · 1,2-ethanediol · additive · 8 copies · chains A
ACT · Acetate ion · additive

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	274	0.63	0.80	35	EDO
2	58	0.35	0.77	14	EDO

Compared structures

5D2G · 4-oxalocrotonate decarboxylase from Pseudomonas putida G7 - complexed with magnesium · 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 Q1XGK3
Elsewhere: RCSB PDB 5D2G · PDBe 5D2G · UniProt Q1XGK3

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