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Dihydrodipicolinate synthase (dhdps) from C.JEJUNI, H59K mutant with pyruvate bound in the active site in C2221 space group

Analyse Dihydrodipicolinate synthase (dhdps) from C.JEJUNI, H59K mutant with pyruvate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7LBD
Type: protein
Length: 1,776 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q9PPB4
Ligands: MG

Structure

x-ray diffraction · 1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F	—	protein	296	—	Q9PPB4

Ligands and binding sites

MG · Magnesium ion · metal · 6 copies · chains A, B, C
EDO · 1,2-ethanediol · additive · 16 copies · chains A, D, B, C, E, F
ACT · Acetate ion · additive · 10 copies · chains A, C, D, E
PEG · Di(hydroxyethyl)ether · additive · 9 copies · chains A, D, B, C, F
PGE · Triethylene glycol · additive · 6 copies · chains A, B, C, D, E

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

Compared structures

7LBD · Dihydrodipicolinate synthase (DHDPS) from C.jejuni, H59K mutant with pyruvate bound in… · the same entry in another collection · chain F against F, TM-score 1.00
Q9PPB4 · AlphaFold monomer V2.0 prediction for 4-hydroxy- tetrahydrodipicolinate synthase (Q9PPB4) · a predicted model of the same protein · chain B 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 Q9PPB4
Elsewhere: RCSB PDB 7LBD · PDBe 7LBD · UniProt Q9PPB4

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