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The crystal structure of corynebacterium glutamicum dihydrodipicolinate synthase to 2.2 a resolution

Analyse The crystal structure of corynebacterium glutamicum dihydrodipicolinate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3CPR
Type
protein
Length
604 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Dihydrodipicolinate synthetase
EC
4.2.1.52
UniProt
Q546B6
Pockets
3 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BDihydrodipicolinate synthetase (EC 4.2.1.52)protein30250% helix, 13% strandQ546B6

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14430.690.8052empty
21980.570.8042empty
31730.540.8038empty

Interfaces

1 interface between chains.

  • A–B · 1272 Ų buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (nonstandard).

Compared structures

  • 3CPR · The crystal structure of Corynebacterium glutamicum dihydrodipicolinate synthase to 2.2 A… · the same entry in another collection · chain A against A, TM-score 1.00

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