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Crystal structure of dihydrodipicolinate synthase from bacillus clausii

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

PDB: 3E96
Type: protein
Length: 596 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dihydrodipicolinate synthase
EC: 4.2.1.52
UniProt: Q5WDL1
Pockets: 5 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 47% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dihydrodipicolinate synthase (EC 4.2.1.52)	protein	296	49% helix, 13% strand	Q5WDL1
B	Dihydrodipicolinate synthase (EC 4.2.1.52)	protein	300	46% helix, 13% strand	Q5WDL1

Pockets

5 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	884	0.77	0.80	90	empty
2	141	0.40	0.74	31	empty
3	64	0.40	0.80	14	empty
4	104	0.35	0.74	29	empty
5	66	0.32	0.76	14	empty

Interfaces

1 interface between chains.

A–B · 1531 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

3E96 · Crystal structure of dihydrodipicolinate synthase from bacillus clausii · 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 Q5WDL1
Elsewhere: RCSB PDB 3E96 · PDBe 3E96 · UniProt Q5WDL1

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