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Transpeptidase domain of FTSI4 D,D-transpeptidase from legionella pneumophila.

Analyse Transpeptidase domain of FTSI4 D,D-transpeptidase from legionella pneumophila. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4ZTK
Type: protein
Length: 268 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cell division protein FTSI/PENICILLIN binding protein 2
UniProt: G8UTM2
Pockets: 1 · best druggability 0.26

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cell division protein FTSI/PENICILLIN binding protein 2	protein	268	44% helix, 20% strand	G8UTM2

Ligands and binding sites

NHE · 2-[N-cyclohexylamino]ethane sulfonic acid · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	56	0.26	0.73	20	NHE

Modifications

Observed in the structure: 5 modified (engineered).

Compared structures

4ZTK · Transpeptidase domain of FtsI4 D,D-transpeptidase from Legionella pneumophila. · 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 G8UTM2
Elsewhere: RCSB PDB 4ZTK · PDBe 4ZTK · UniProt G8UTM2

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