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Crystal structure of dihydrodipicolinate synthase from oceanobacillus iheyensis at 1.9 a resolution

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

PDB: 3D0C
Type: protein
Length: 602 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dihydrodipicolinate synthase
EC: 4.2.1.52
UniProt: Q8EMJ7
Pockets: 3 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 55% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dihydrodipicolinate synthase (EC 4.2.1.52)	protein	302	55% helix, 12% strand	Q8EMJ7
B	Dihydrodipicolinate synthase (EC 4.2.1.52)	protein	300	55% helix, 12% strand	Q8EMJ7

Pockets

3 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	908	0.78	0.81	80	empty
2	80	0.33	0.74	14	empty
3	55	0.28	0.74	16	empty

Interfaces

1 interface between chains.

A–B · 1682 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

3D0C · Crystal structure of dihydrodipicolinate synthase from Oceanobacillus iheyensis at 1.9 A… · 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 Q8EMJ7
Elsewhere: RCSB PDB 3D0C · PDBe 3D0C · UniProt Q8EMJ7

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