Research workbench

Acinetobacter baumannii ribosome-tigecycline complex - 50S subunit

Analyse Acinetobacter baumannii ribosome-tigecycline complex - 50S subunit in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6YSI
Type: protein + RNA
Length: 5,912 residues
Chains: 32
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: D0CD00, D0CCZ7, D0CCZ8, D0CD09, D0CD12, D0CG35, D0CD07, D0CD16, D0CD04, D0CD23, D0CD13, D0CCR8, D0CA76, D0CDQ6, D0CD02, D0CCZ9, D0CD08, D0C9L7, D0CDQ7, D0CAL0, D0CD05, D0CD15, D0CBZ8, D0C9K5, D0CAL1, D0CG06, D0CA77, D0CD18
Ligands: T1C, MG, ZN

Structure

electron microscopy · 32 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	272	—	D0CD00
B	—	protein	211	—	D0CCZ7
C	—	protein	199	—	D0CCZ8
D	—	protein	176	—	D0CD09
E	—	protein	175	—	D0CD12
F	—	protein	142	—	D0CG35
G	—	protein	122	—	D0CD07
H	—	protein	144	—	D0CD16
I	—	protein	137	—	D0CD04
J	—	protein	119	—	D0CD23
K	—	protein	115	—	D0CD13
L	—	protein	117	—	D0CCR8
M	—	protein	117	—	D0CA76
N	—	protein	103	—	D0CDQ6
O	—	protein	109	—	D0CD02
P	—	protein	92	—	D0CCZ9
Q	—	protein	102	—	D0CD08
R	—	protein	96	—	D0C9L7
S	—	protein	76	—	D0CDQ7
T	—	protein	77	—	D0CAL0
U	—	protein	61	—	D0CD05
V	—	protein	57	—	D0CD15
W	—	protein	43	—	D0CBZ8
X	—	protein	54	—	D0C9K5
Y	—	protein	51	—	D0CAL1
Z	—	protein	44	—	D0CG06
1	—	rna	2672	—	—
5	—	rna	115	—	—
6	—	rna	5	—	—
8	—	rna	8	—	—
a	—	protein	63	—	D0CA77
b	—	protein	38	—	D0CD18

Ligands and binding sites

T1C · Tigecycline · ligand · 3 copies · chains S, 1, 5, K
MG · Magnesium ion · metal · 162 copies · chains 1, A, B, F, J, 5
ZN · Zinc ion · metal · chains b

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

Compared structures

6YSI · Acinetobacter baumannii ribosome-tigecycline complex - 50S subunit · the same entry in another collection · chain B against B, 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 D0CD00
Every structure of UniProt D0CCZ7
Every structure of UniProt D0CCZ8
Every structure of UniProt D0CD09
Every structure of UniProt D0CD12
Every structure of UniProt D0CG35
Every structure of UniProt D0CD07
Every structure of UniProt D0CD16
Every structure of UniProt D0CD04
Every structure of UniProt D0CD23
Every structure of UniProt D0CD13
Every structure of UniProt D0CCR8
Every structure of UniProt D0CA76
Every structure of UniProt D0CDQ6
Every structure of UniProt D0CD02
Every structure of UniProt D0CCZ9
Every structure of UniProt D0CD08
Every structure of UniProt D0C9L7
Every structure of UniProt D0CDQ7
Every structure of UniProt D0CAL0
Every structure of UniProt D0CD05
Every structure of UniProt D0CD15
Every structure of UniProt D0CBZ8
Every structure of UniProt D0C9K5
Every structure of UniProt D0CAL1
Every structure of UniProt D0CG06
Every structure of UniProt D0CA77
Every structure of UniProt D0CD18
Elsewhere: RCSB PDB 6YSI · PDBe 6YSI · UniProt D0CD00 · UniProt D0CCZ7 · UniProt D0CCZ8 · UniProt D0CD09 · UniProt D0CD12 · UniProt D0CG35 · UniProt D0CD07 · UniProt D0CD16 · UniProt D0CD04 · UniProt D0CD23 · UniProt D0CD13 · UniProt D0CCR8 · UniProt D0CA76 · UniProt D0CDQ6 · UniProt D0CD02 · UniProt D0CCZ9 · UniProt D0CD08 · UniProt D0C9L7 · UniProt D0CDQ7 · UniProt D0CAL0 · UniProt D0CD05 · UniProt D0CD15 · UniProt D0CBZ8 · UniProt D0C9K5 · UniProt D0CAL1 · UniProt D0CG06 · UniProt D0CA77 · UniProt D0CD18

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