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Crystal structure of the apo forms of rhodotorula graminis D-mandelate dehydrogenase at 1.8A.

Analyse Crystal structure of the apo forms of rhodotorula graminis D-mandelate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2W2K
Type
protein
Length
689 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
D-mandelate dehydrogenase
UniProt
Q7LLW9
Pockets
2 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 41% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AD-mandelate dehydrogenaseprotein34541% helix, 16% strandQ7LLW9
BD-mandelate dehydrogenaseprotein34441% helix, 16% strandQ7LLW9

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17580.740.7966empty
27390.710.7862empty

Interfaces

1 interface between chains.

  • A–B · 2765 Ų buried · 35 hydrogen bonds · protein-protein

Compared structures

  • 2W2K · Crystal structure of the apo forms of Rhodotorula graminis D- mandelate dehydrogenase at… · the same entry in another collection · chain A against A, TM-score 1.00

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