Research workbench

50S deinococcus radiodurans ribosome bounded with mycinamicin IV

Analyse 50S deinococcus radiodurans ribosome bounded with mycinamicin IV in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7A18
Type: protein + RNA
Length: 5,915 residues
Chains: 28
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: RNA (2699-mer); RNA (122-mer); 50S ribosomal protein L2; 50S ribosomal protein L3; 50S…
UniProt: Q9RXJ9, Q9RXK2, Q9RXK1, Q9RXJ0, Q9RSL3, Q9RXY1, Q9RXJ2, Q9RSK9, Q9RXJ5, Q9RSJ5, Q9RSL2, Q9RWB4, Q9RSW7, Q9RY64, Q9RXJ7, Q9RXK0, Q9RXJ1, Q9RX88, Q9RY65, Q9RRG8, Q9RXJ4, Q9RSL0, P49228, Q9RSS4, Q9RSH2, Q9RSW6
Ligands: SPD, MIV, MG
Pockets: 20 · best druggability 0.89

Structure

x-ray diffraction · 28 distinct chains · 22% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
X	RNA (2699-mer)	rna	2699	—	—
Y	RNA (122-mer)	rna	122	—	—
A	50S ribosomal protein L2	protein	271	4% helix, 21% strand	Q9RXJ9
B	50S ribosomal protein L3	protein	206	12% helix, 40% strand	Q9RXK2
C	50S ribosomal protein L4	protein	195	26% helix, 7% strand	Q9RXK1
D	50S ribosomal protein L5	protein	176	29% helix, 18% strand	Q9RXJ0
E	50S ribosomal protein L6	protein	171	22% helix, 29% strand	Q9RSL3
G	50S ribosomal protein L13	protein	142	30% helix, 11% strand	Q9RXY1
H	50S ribosomal protein L14	protein	134	7% helix, 37% strand	Q9RXJ2
I	50S ribosomal protein L15	protein	137	12% helix, 9% strand	Q9RSK9
J	50S ribosomal protein L16	protein	134	19% helix, 23% strand	Q9RXJ5
K	50S ribosomal protein L17	protein	115	51% helix, 16% strand	Q9RSJ5
L	50S ribosomal protein L18	protein	104	37% helix, 8% strand	Q9RSL2
M	50S ribosomal protein L19	protein	118	14% helix, 34% strand	Q9RWB4
N	50S ribosomal protein L20	protein	117	74% helix, 0% strand	Q9RSW7
O	50S ribosomal protein L21	protein	98	3% helix, 42% strand	Q9RY64
P	50S ribosomal protein L22	protein	129	38% helix, 34% strand	Q9RXJ7
Q	50S ribosomal protein L23	protein	93	19% helix, 35% strand	Q9RXK0
R	50S ribosomal protein L24	protein	110	0% helix, 31% strand	Q9RXJ1
S	50S ribosomal protein L25	protein	174	14% helix, 28% strand	Q9RX88
T	50S ribosomal protein L27	protein	72	0% helix, 33% strand	Q9RY65
U	50S ribosomal protein L28	protein	74	14% helix, 11% strand	Q9RRG8
V	50S ribosomal protein L29	protein	54	76% helix, 0% strand	Q9RXJ4
W	50S ribosomal protein L30	protein	55	38% helix, 15% strand	Q9RSL0
Z	50S ribosomal protein L32	protein	57	14% helix, 14% strand	P49228
1	50S ribosomal protein L33	protein	49	0% helix, 31% strand	Q9RSS4
2	50S ribosomal protein L34	protein	46	52% helix, 0% strand	Q9RSH2
3	50S ribosomal protein L35	protein	63	22% helix, 10% strand	Q9RSW6

Ligands and binding sites

SPD · Spermidine · ligand · 7 copies · chains X, H, K, N, V
MIV · Mycinamicin IV · ligand · chains X
MG · Magnesium ion · metal · 277 copies · chains X, A, O, M, N, P, G, K, Z, I, C, J, B, T, Y, Q, W, 2, 3

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

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	978	0.89	0.91	94	MG
2	857	0.88	0.91	87	MG
3	947	0.87	0.90	96	MG
4	1044	0.87	0.89	101	MG
5	867	0.87	0.90	77	MG

Interfaces

53 interfaces between chains.

X–A · 6758 Å² buried · 155 hydrogen bonds · protein-nucleic
X–B · 5090 Å² buried · 120 hydrogen bonds · protein-nucleic
X–N · 4142 Å² buried · 87 hydrogen bonds · protein-nucleic
X–C · 4112 Å² buried · 84 hydrogen bonds · protein-nucleic
X–I · 4103 Å² buried · 71 hydrogen bonds · protein-nucleic

Modifications

Observed in the structure: 8 covalent, 1 disulfide (covalent ligand, disulfide).

Compared structures

7A18 · 50S Deinococcus radiodurans ribosome bounded with mycinamicin IV · the same entry in another collection · chain J against J, 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 Q9RXJ9
Every structure of UniProt Q9RXK2
Every structure of UniProt Q9RXK1
Every structure of UniProt Q9RXJ0
Every structure of UniProt Q9RSL3
Every structure of UniProt Q9RXY1
Every structure of UniProt Q9RXJ2
Every structure of UniProt Q9RSK9
Every structure of UniProt Q9RXJ5
Every structure of UniProt Q9RSJ5
Every structure of UniProt Q9RSL2
Every structure of UniProt Q9RWB4
Every structure of UniProt Q9RSW7
Every structure of UniProt Q9RY64
Every structure of UniProt Q9RXJ7
Every structure of UniProt Q9RXK0
Every structure of UniProt Q9RXJ1
Every structure of UniProt Q9RX88
Every structure of UniProt Q9RY65
Every structure of UniProt Q9RRG8
Every structure of UniProt Q9RXJ4
Every structure of UniProt Q9RSL0
Every structure of UniProt P49228
Every structure of UniProt Q9RSS4
Every structure of UniProt Q9RSH2
Every structure of UniProt Q9RSW6
Elsewhere: RCSB PDB 7A18 · PDBe 7A18 · UniProt Q9RXJ9 · UniProt Q9RXK2 · UniProt Q9RXK1 · UniProt Q9RXJ0 · UniProt Q9RSL3 · UniProt Q9RXY1 · UniProt Q9RXJ2 · UniProt Q9RSK9 · UniProt Q9RXJ5 · UniProt Q9RSJ5 · UniProt Q9RSL2 · UniProt Q9RWB4 · UniProt Q9RSW7 · UniProt Q9RY64 · UniProt Q9RXJ7 · UniProt Q9RXK0 · UniProt Q9RXJ1 · UniProt Q9RX88 · UniProt Q9RY65 · UniProt Q9RRG8 · UniProt Q9RXJ4 · UniProt Q9RSL0 · UniProt P49228 · UniProt Q9RSS4 · UniProt Q9RSH2 · UniProt Q9RSW6

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.