Research workbench

1.30 a crystal structure of dape enzyme from neisseria meningitidis MC58

Analyse 1.30 a crystal structure of dape enzyme from neisseria meningitidis MC58 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5UEJ
Type: protein
Length: 751 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q9JYL2
Ligands: ZN, SO4

Structure

x-ray diffraction · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	375	—	Q9JYL2
B	—	protein	376	—	Q9JYL2

Ligands and binding sites

ZN · Zinc ion · metal · 5 copies · chains A, B
SO4 · Sulfate ion · ion · 5 copies · chains A, B

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

Compared structures

5UEJ · 1.30 A crystal structure of DapE enzyme from Neisseria meningitidis MC58 · the same entry in another collection · chain A against A, TM-score 1.00
Q9JYL2 · AlphaFold monomer V2.0 prediction for succinyl-diaminopimelate desuccinylase (Q9JYL2) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q9JYL2
Elsewhere: RCSB PDB 5UEJ · PDBe 5UEJ · UniProt Q9JYL2

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.