MolNFT v1 · #179990 · protein

Dihydrodipicolinate synthase (dhdps) from C.JEJUNI, H59A mutant with pyruvate bound in the active site and R,R-bislysine bound at the allosteric site

7KM0: “Dihydrodipicolinate synthase (dhdps) from C.JEJUNI, H59A mutant with pyruvate bound in the active site and…”. X-ray diffraction, 2 ligands (3VN, MG). MolNFT v1 #179990 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7KM0
Type: protein
Length: 1,776 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q9PPB4
Ligands: 3VN, 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

3VN · (2R,5R)-2,5-diamino-2,5-bis(4-aminobutyl)hexanedioic acid · ligand · 3 copies · chains B, C, A, D, E, F
MG · Magnesium ion · metal · chains A
EDO · 1,2-ethanediol · additive · 5 copies · chains A, B, D
PEG · Di(hydroxyethyl)ether · additive · 3 copies · chains A, D, C
ACT · Acetate ion · additive · chains A
PGE · Triethylene glycol · additive · chains B

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

Compared structures

7KM0 · Dihydrodipicolinate synthase (DHDPS) from C.jejuni, H59A 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 7KM0 · PDBe 7KM0 · UniProt Q9PPB4

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