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MolNFT v1 · #161968 · protein + RNA

Structure of a bacterial 50S ribosomal subunit in complex with the novel quinoxolidinone antibiotic cadazolid

6QUL: “Structure of a bacterial 50S ribosomal subunit in complex with the novel quinoxolidinone antibiotic cadazolid”. Electron microscopy, 4 ligands (FME, JJH, MG). MolNFT v1 #161968 on GenesisL1: 3D structure, binding sites and pockets…

PDB
6QUL
Type
protein + RNA
Length
6,054 residues
Chains
31
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt
P60422, P60438, P60723, P62399, P0AG55, P0A7R1, P0AA10, P0ADY3, P02413, P0ADY7, P0AG44, P0C018, P0A7K6, P0A7L3, P0AG48, P61175, P0ADZ0, P60624, P68919, P0A7L8, P0A7M2, P0A7M6, P0AG51, P0A7N4, P0A7N9, P0A7P5, P0A7Q1, P0A7Q6
Ligands
FME, JJH, MG, ZN

Structure

electron microscopy · 31 distinct chains.

ChainMoleculeTypeResiduesSecondary structureUniProt
1—rna4——
A—rna2796——
B—rna120——
C—protein271—P60422
D—protein209—P60438
E—protein201—P60723
F—protein177—P62399
G—protein176—P0AG55
H—protein50—P0A7R1
K—protein142—P0AA10
L—protein123—P0ADY3
M—protein144—P02413
N—protein136—P0ADY7
O—protein125—P0AG44
P—protein117—P0C018
Q—protein114—P0A7K6
R—protein117—P0A7L3
S—protein103—P0AG48
T—protein110—P61175
U—protein95—P0ADZ0
V—protein102—P60624
W—protein94—P68919
X—protein76—P0A7L8
Y—protein77—P0A7M2
Z—protein62—P0A7M6
a—protein58—P0AG51
b—protein56—P0A7N4
c—protein51—P0A7N9
d—protein46—P0A7P5
e—protein64—P0A7Q1
f—protein38—P0A7Q6

Ligands and binding sites

  • FME · N-formylmethionine · ligand · chains 1, A
  • JJH · cadazolid · ligand · chains 1, A
  • MG · Magnesium ion · metal · 382 copies · chains 1, A, M, C, O, U, D, c, K, B, b
  • ZN · Zinc ion · metal · chains f

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

Compared structures

  • 6QUL · Structure of a bacterial 50S ribosomal subunit in complex with the novel quinoxolidi… · the same entry in another collection · chain 1 against 1, TM-score 1.00

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