MolNFT v1 · #123521 · protein

The crystal structure of the catalytic domain of peptidoglycan N- acetylglucosamine deacetylase from eubacterium rectale atcc 33656

5JMU · Peptidoglycan N-acetylglucosamine deacetylase: “The crystal structure of the catalytic domain of peptidoglycan N- acetylglucosamine deacetylase from…”. X-ray diffraction, 2 ligands (ZN, MG), 2 pockets (best druggability 0.30).…

PDB: 5JMU
Type: protein
Length: 220 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peptidoglycan N-acetylglucosamine deacetylase
UniProt: C4ZEZ9
Ligands: ZN, MG
Pockets: 2 · best druggability 0.30

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peptidoglycan N-acetylglucosamine deacetylase	protein	220	40% helix, 15% strand	C4ZEZ9

Ligands and binding sites

ZN · Zinc ion · metal · chains A
MG · Magnesium ion · metal · chains A
ACT · Acetate ion · additive · chains A

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	74	0.30	0.73	16	empty
2	52	0.28	0.75	14	empty

Modifications

Observed in the structure: 5 modified (engineered, oxidation).

Compared structures

5JMU · The crystal structure of the catalytic domain of peptidoglycan N-acetylglucosamine… · 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 C4ZEZ9
Elsewhere: RCSB PDB 5JMU · PDBe 5JMU · UniProt C4ZEZ9

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