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Crystal structure of dihydrodipicolinate synthase from rhodopseudomonas palustris at 2.0A resolution

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

PDB
3EB2
Type
protein
Length
1,157 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Putative dihydrodipicolinate synthetase
EC
4.2.1.52
UniProt
Q6N9H8
Pockets
16 · best druggability 0.78

Structure

x-ray diffraction · 3 distinct chains · 51% helix, 14% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CPutative dihydrodipicolinate synthetase (EC 4.2.1.52)protein28851% helix, 15% strandQ6N9H8
BPutative dihydrodipicolinate synthetase (EC 4.2.1.52)protein29151% helix, 14% strandQ6N9H8
DPutative dihydrodipicolinate synthetase (EC 4.2.1.52)protein29050% helix, 14% strandQ6N9H8

Ligands and binding sites

  • PGE · Triethylene glycol · additive · 2 copies · chains A, C, B, D

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

Pockets

16 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15870.780.8477empty
25480.770.8475empty
3670.720.9719empty
4570.720.9818empty
5540.710.9818empty

Interfaces

4 interfaces between chains.

  • B–D · 1309 Ų buried · 10 hydrogen bonds · protein-protein
  • A–C · 1303 Ų buried · 10 hydrogen bonds · protein-protein
  • C–D · 1106 Ų buried · 12 hydrogen bonds · protein-protein
  • A–B · 1085 Ų buried · 12 hydrogen bonds · protein-protein

Compared structures

  • 3EB2 · Crystal structure of Dihydrodipicolinate Synthase from Rhodopseudomonas palustris at 2.0A… · the same entry in another collection · chain A against A, TM-score 1.00

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