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

Analyse Crystal structure of the mutant E234A of galacturonate dehydratase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

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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