MolNFT v1 · #159541 · protein

Crystal structure of the D-alanyl-D-alanine carboxypeptidase dacd from francisella tularensis

6OSU · D-alanyl-D-alanine carboxypeptidase (penicillin binding…: “Crystal structure of the D-alanyl-D-alanine carboxypeptidase dacd from francisella tularensis”. X-ray diffraction, 1 ligand (CL), 2 pockets (best druggability 0.43). MolNFT…

PDB: 6OSU
Type: protein
Length: 413 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: D-alanyl-D-alanine carboxypeptidase (penicillin binding protein) family protein
EC: 3.4.16.4
UniProt: Q5NG28
Ligands: CL
Pockets: 2 · best druggability 0.43

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	D-alanyl-D-alanine carboxypeptidase (penicillin binding protein) family protein (EC 3.4.16.4)	protein	413	31% helix, 29% strand	Q5NG28

Ligands and binding sites

CL · Chloride ion · ion · chains A
EDO · 1,2-ethanediol · 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	97	0.43	0.79	27	EDO
2	101	0.36	0.74	21	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

6OSU · Crystal Structure of the D-alanyl-D-alanine carboxypeptidase DacD from Francisella… · 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 Q5NG28
Elsewhere: RCSB PDB 6OSU · PDBe 6OSU · UniProt Q5NG28

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