MolNFT v1 · #179233 · protein

Dihydrodipicolinate synthase mutation S48W with lysine in the allosteric site

7JZD · 4-hydroxy-tetrahydrodipicolinate synthase: “Dihydrodipicolinate synthase mutation S48W with lysine in the allosteric site”. X-ray diffraction, 1 ligand (K), 3 pockets (best druggability 0.72). MolNFT v1 #179233 on GenesisL1: 3D…

PDB: 7JZD
Type: protein
Length: 584 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 4-hydroxy-tetrahydrodipicolinate synthase
EC: 4.3.3.7
UniProt: A0A066Q637
Ligands: K
Pockets: 3 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	4-hydroxy-tetrahydrodipicolinate synthase (EC 4.3.3.7)	protein	292	46% helix, 13% strand	A0A066Q637

Ligands and binding sites

K · Potassium ion · metal · 2 copies · chains A, B
GOL · Glycerol · additive · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	423	0.72	0.82	47	empty
2	133	0.54	0.81	24	GOL
3	141	0.49	0.79	30	GOL

Interfaces

1 interface between chains.

A–B · 1310 Å² buried · 16 hydrogen bonds · protein-protein

Compared structures

7JZD · Dihydrodipicolinate synthase mutation S48W with Lysine in the allosteric site · 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 A0A066Q637
Elsewhere: RCSB PDB 7JZD · PDBe 7JZD · UniProt A0A066Q637

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