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Crystal structure of D-mannonate dehydratase from novosphingobium aromaticivorans mutant (V161A, R163A, K165G, L166A, Y167G, Y168A, E169G)

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

PDB: 4K8G
Type: protein
Length: 386 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mandelate RACEMASE/MUCONATE lactonizing enzyme, N-terminal domain protein
UniProt: A4XF23
Ligands: MG
Pockets: 1 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mandelate RACEMASE/MUCONATE lactonizing enzyme, N-terminal domain protein	protein	386	40% helix, 20% strand	A4XF23

Ligands and binding sites

MG · Magnesium ion · metal · chains A
GOL · Glycerol · additive · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	613	0.68	0.77	68	GOL

Compared structures

4K8G · Crystal structure of D-Mannonate dehydratase from Novosphingobium aromaticivorans mutant… · the same entry in another collection · chain A against A, TM-score 1.00
A4XF23 · AlphaFold monomer V2.0 prediction for D-mannonate dehydratase (A4XF23) · a predicted model of the same protein · 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 A4XF23
Elsewhere: RCSB PDB 4K8G · PDBe 4K8G · UniProt A4XF23

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