MolNFT v1 · #30685 · protein

Dihydrodipicolinate synthase (E. COLI)- mutant R138H

2A6L: “Dihydrodipicolinate synthase (E. COLI)- mutant R138H”. X-ray diffraction, 1 ligand (K), 3 pockets (best druggability 0.72). MolNFT v1 #30685 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2A6L
Type: protein
Length: 584 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dihydrodipicolinate synthase
EC: 4.2.1.52
UniProt: P0A6L2
Ligands: K
Pockets: 3 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Dihydrodipicolinate synthase (EC 4.2.1.52)	protein	292	45% helix, 13% strand	P0A6L2

Ligands and binding sites

K · Potassium ion · metal · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	378	0.72	0.83	56	empty
2	121	0.49	0.80	24	empty
3	110	0.48	0.80	22	empty

Interfaces

1 interface between chains.

A–B · 1328 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

2A6L · Dihydrodipicolinate synthase (E. coli)- mutant R138H · the same entry in another collection · chain A against A, TM-score 1.00
P0A6L2 · AlphaFold monomer V2.0 prediction for 4-hydroxy- tetrahydrodipicolinate synthase (P0A6L2) · a predicted model of the same protein · 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 P0A6L2
Elsewhere: RCSB PDB 2A6L · PDBe 2A6L · UniProt P0A6L2

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