Research workbench

50S ribosomal subunit from Staphylococcus aureus containing double mutation in uL3 imparting linezolid resistance

Analyse 50S ribosomal subunit from Staphylococcus aureus containing double mutation in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7TTW
Type: protein + RNA
Length: 5,462 residues
Chains: 27
Method: electron microscopy
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.9
Source: Staphylococcus aureus
Molecule: 50S ribosomal protein L19; 50S ribosomal protein L2; 50S ribosomal protein L20; 50S…
UniProt: A0A077UVB6, A0A077W1J0, A0A077VMP6, D7URR3, A0A0D1H5C2, W8TUB4, W8TRD5, A0A133Q8Z9, A0A0D1H0B5, A0A077URJ8, A0A7R6P2U0, A0A0D1GR95, W8UVN7, A0A077UWR7, A0A077UXT4, Q2YZB6, A0A0D1H088, A0A077UGV8, A0A166DK89, W8TUE6, A0A077UUA0, A0A077UGA7, A0A077V4G0, A0A077UG91, W8TRE0
Pockets: 20 · best druggability 0.88

Structure

electron microscopy · resolution 2.9 · 27 distinct chains · 22% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	50S ribosomal protein L19	protein	113	13% helix, 42% strand	A0A077UVB6
B	50S ribosomal protein L2	protein	273	7% helix, 28% strand	A0A077W1J0
C	50S ribosomal protein L20	protein	116	75% helix, 0% strand	A0A077VMP6
D	50S ribosomal protein L21	protein	100	0% helix, 51% strand	D7URR3
E	50S ribosomal protein L22	protein	111	37% helix, 35% strand	A0A0D1H5C2
F	50S ribosomal protein L23	protein	87	24% helix, 44% strand	W8TUB4
G	50S ribosomal protein L24	protein	90	3% helix, 40% strand	W8TRD5
H	50S ribosomal protein L25	protein	93	22% helix, 47% strand	A0A133Q8Z9
I	50S ribosomal protein L27	protein	78	0% helix, 37% strand	A0A0D1H0B5
J	50S ribosomal protein L28	protein	59	5% helix, 37% strand	A0A077URJ8
K	50S ribosomal protein L29	protein	61	66% helix, 0% strand	A0A7R6P2U0
L	50S ribosomal protein L3	protein	215	9% helix, 38% strand	A0A0D1GR95
M	50S ribosomal protein L30	protein	56	30% helix, 25% strand	W8UVN7
N	50S ribosomal protein L32	protein	50	14% helix, 12% strand	A0A077UWR7
O	50S ribosomal protein L33	protein	47	0% helix, 53% strand	A0A077UXT4
P	50S ribosomal protein L34	protein	44	57% helix, 0% strand	Q2YZB6
Q	50S ribosomal protein L35	protein	64	31% helix, 11% strand	A0A0D1H088
R	50S ribosomal protein L36	protein	37	8% helix, 27% strand	A0A077UGV8
S	50S ribosomal protein L4	protein	192	33% helix, 9% strand	A0A166DK89
V	50S ribosomal protein L13	protein	143	28% helix, 19% strand	W8TUE6
W	50S ribosomal protein L14	protein	121	7% helix, 36% strand	A0A077UUA0
X	50S ribosomal protein L15	protein	144	14% helix, 12% strand	A0A077UGA7
Y	50S ribosomal protein L16	protein	136	18% helix, 27% strand	A0A077V4G0
Z	50S ribosomal protein L17	protein	121	45% helix, 20% strand	A0A077UG91
a	50S ribosomal protein L18	protein	110	30% helix, 22% strand	W8TRE0
1	23S rRNA	rna	2690	—	—
2	5S rRNA	rna	111	—	—

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	1046	0.88	0.91	88	empty
2	958	0.88	0.90	102	empty
3	485	0.86	0.93	56	empty
4	442	0.85	0.93	62	empty
5	823	0.85	0.88	75	empty

Interfaces

51 interfaces between chains.

B–1 · 6920 Å² buried · 126 hydrogen bonds · protein-nucleic
L–1 · 4944 Å² buried · 88 hydrogen bonds · protein-nucleic
X–1 · 4347 Å² buried · 83 hydrogen bonds · protein-nucleic
S–1 · 4250 Å² buried · 64 hydrogen bonds · protein-nucleic
C–1 · 3985 Å² buried · 71 hydrogen bonds · protein-nucleic

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

7TTW · 50S ribosomal subunit from staphylococcus aureus containing double mutation in UL3… · the same entry in another collection · chain 1 against 1, 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 A0A077UVB6
Every structure of UniProt A0A077W1J0
Every structure of UniProt A0A077VMP6
Every structure of UniProt D7URR3
Every structure of UniProt A0A0D1H5C2
Every structure of UniProt W8TUB4
Every structure of UniProt W8TRD5
Every structure of UniProt A0A133Q8Z9
Every structure of UniProt A0A0D1H0B5
Every structure of UniProt A0A077URJ8
Every structure of UniProt A0A7R6P2U0
Every structure of UniProt A0A0D1GR95
Every structure of UniProt W8UVN7
Every structure of UniProt A0A077UWR7
Every structure of UniProt A0A077UXT4
Every structure of UniProt Q2YZB6
Every structure of UniProt A0A0D1H088
Every structure of UniProt A0A077UGV8
Every structure of UniProt A0A166DK89
Every structure of UniProt W8TUE6
Every structure of UniProt A0A077UUA0
Every structure of UniProt A0A077UGA7
Every structure of UniProt A0A077V4G0
Every structure of UniProt A0A077UG91
Every structure of UniProt W8TRE0
Elsewhere: RCSB PDB 7TTW · PDBe 7TTW · UniProt A0A077UVB6 · UniProt A0A077W1J0 · UniProt A0A077VMP6 · UniProt D7URR3 · UniProt A0A0D1H5C2 · UniProt W8TUB4 · UniProt W8TRD5 · UniProt A0A133Q8Z9 · UniProt A0A0D1H0B5 · UniProt A0A077URJ8 · UniProt A0A7R6P2U0 · UniProt A0A0D1GR95 · UniProt W8UVN7 · UniProt A0A077UWR7 · UniProt A0A077UXT4 · UniProt Q2YZB6 · UniProt A0A0D1H088 · UniProt A0A077UGV8 · UniProt A0A166DK89 · UniProt W8TUE6 · UniProt A0A077UUA0 · UniProt A0A077UGA7 · UniProt A0A077V4G0 · UniProt A0A077UG91 · UniProt W8TRE0

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