MolNFT v1 · #81870 · protein

Crystal structure of the mutant E234A of galacturonate dehydratase from geobacillus sp. complexed with mg

3V5F · Mandelate RACEMASE/MUCONATE lactonizing protein: “Crystal structure of the mutant E234A of galacturonate dehydratase from geobacillus sp. complexed with mg”. X-ray diffraction, 1 ligand (MG), 2 pockets (best druggability 0.52).…

PDB: 3V5F
Type: protein
Length: 386 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mandelate RACEMASE/MUCONATE lactonizing protein
UniProt: D3EID5
Ligands: MG
Pockets: 2 · best druggability 0.52

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mandelate RACEMASE/MUCONATE lactonizing protein	protein	386	35% helix, 26% strand	D3EID5

Ligands and binding sites

MG · Magnesium ion · metal · 2 copies · chains A
EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 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	61	0.52	0.86	19	empty
2	176	0.47	0.76	30	MG

Compared structures

3V5F · Crystal structure of the mutant E234A of Galacturonate Dehydratase from GEOBACILLUS SP.… · 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 D3EID5
Elsewhere: RCSB PDB 3V5F · PDBe 3V5F · UniProt D3EID5

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