MolNFT v1 · #103488 · protein

Crystal structure of S. aureus autolysin E in complex with muropeptide nam-L-ala-D-iglu

4PI9: “Crystal structure of S. aureus autolysin E in complex with muropeptide nam-L-ala-D-iglu”. X-ray diffraction, 3 ligands (3LT, CL, SO4), 1 pocket (best druggability 0.31). MolNFT v1 #103488 on GenesisL1: 3D structure, binding sites…

PDB: 4PI9
Type: protein
Length: 222 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Autolysin E
UniProt: A0A0H3JT72
Ligands: 3LT, CL, SO4
Pockets: 1 · best druggability 0.31

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Autolysin E	protein	222	48% helix, 8% strand	A0A0H3JT72

Ligands and binding sites

3LT · (4R)-4-[[(2S)-2-[[(2R)-2-[(2R,3S,4R,5R,6R)-5-acetamido-2-(hydroxymethyl)-3,6-bis(oxidanyl)oxan-4-yl]oxypropanoyl]amino]propanoyl]amino]-5-azanyl-5-oxidanylidene-pentanoic acid · ligand · chains A
CL · Chloride ion · ion · 7 copies · chains A
SO4 · Sulfate ion · ion · 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	68	0.31	0.74	23	SO4

Compared structures

4PI9 · Crystal structure of S. Aureus Autolysin E in complex with muropeptide NAM-L-ALA-D-iGLU · 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 A0A0H3JT72
Elsewhere: RCSB PDB 4PI9 · PDBe 4PI9 · UniProt A0A0H3JT72

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