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Crystal and cryoem structural studies of a cell wall degrading enzyme in the bacteriophage PHI29 tail

Analyse Crystal and cryoem structural studies of a cell wall degrading enzyme in the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3CSZ
Type: protein
Length: 159 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Morphogenesis protein 1
UniProt: P15132
Ligands: NAG
Pockets: 1 · best druggability 0.29

Structure

x-ray diffraction · 1 distinct chain · 55% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Morphogenesis protein 1	protein	159	55% helix, 2% strand	P15132

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · 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	54	0.29	0.75	18	NAG

Compared structures

3CSZ · Crystal and cryoEM structural studies of a cell wall degrading enzyme in the… · 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 P15132
Elsewhere: RCSB PDB 3CSZ · PDBe 3CSZ · UniProt P15132

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