MolNFT v1 · #123546 · protein

Mray tunicamycin complex

5JNQ · Phospho-N-acetylmuramoyl-pentapeptide-transferase: “Mray tunicamycin complex”. X-ray diffraction, 2 ligands (PLM, TUM), 2 pockets (best druggability 0.36). MolNFT v1 #123546 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 5JNQ
Type: protein
Length: 307 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phospho-N-acetylmuramoyl-pentapeptide-transferase
EC: 2.7.8.13
UniProt: R0BTE9
Ligands: PLM, TUM
Pockets: 2 · best druggability 0.36

Structure

x-ray diffraction · 1 distinct chain · 74% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phospho-N-acetylmuramoyl-pentapeptide-transferase (EC 2.7.8.13)	protein	307	74% helix, 1% strand	R0BTE9

Ligands and binding sites

PLM · Palmitic acid · ligand · 2 copies · chains A
TUM · Tunicamycin · ligand · chains A
BOG · octyl beta-D-glucopyranoside · 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	73	0.36	0.76	17	empty
2	100	0.35	0.74	25	TUM

Compared structures

5JNQ · MraY tunicamycin complex · 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 R0BTE9
Elsewhere: RCSB PDB 5JNQ · PDBe 5JNQ · UniProt R0BTE9

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