MolNFT v1 · #116068 · protein

4-oxalocrotonate decarboxylase from pseudomonas putida G7 - apo form

5D2F · 4-oxalocrotonate decarboxylase nahk: “4-oxalocrotonate decarboxylase from pseudomonas putida G7 - apo form”. X-ray diffraction, 1 ligand (CL), 3 pockets (best druggability 0.65). MolNFT v1 #116068 on GenesisL1: 3D structure, binding…

PDB: 5D2F
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: CL
Pockets: 3 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	4-oxalocrotonate decarboxylase nahk (EC 4.1.1.77)	protein	263	31% helix, 31% strand	Q1XGK3

Ligands and binding sites

CL · Chloride ion · ion · 2 copies · chains A
EDO · 1,2-ethanediol · additive · 12 copies · chains A
ACT · Acetate ion · additive · chains A

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

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	327	0.65	0.80	36	EDO
2	52	0.32	0.77	15	EDO
3	50	0.29	0.75	13	EDO

Compared structures

5D2F · 4-oxalocrotonate decarboxylase from Pseudomonas putida G7 - apo form · 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 5D2F · PDBe 5D2F · UniProt Q1XGK3

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