Research workbench

Cryo-EM structures of the 50S ribosome subunit bound with obge

Analyse Cryo-EM structures of the 50S ribosome subunit bound with obge in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4CSU
Type: protein + RNA
Length: 6,876 residues
Chains: 33
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 50S ribosomal protein L28; 50S ribosomal protein L29; 50S ribosomal protein L30; 50S…
UniProt: P0A7M2, P0A7M6, P0AG51, P0A7N4, P0A7N9, P0A7L0, P0A7P5, P0A7Q1, P0A7Q6, P42641, P60422, P60438, P60723, P62399, P0AG55, P0A7R1, P0A7J7, P0AA10, P0ADY3, P02413, P0ADY7, P0AG44, P0C018, P0A7K6, P0A7L3, P0AG48, P61175, P0ADZ0, P60624, P68919, P0A7L8
Pockets: 20 · best druggability 0.90

Structure

electron microscopy · 33 distinct chains · 19% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
0	50S ribosomal protein L28	protein	77	22% helix, 16% strand	P0A7M2
1	50S ribosomal protein L29	protein	63	65% helix, 0% strand	P0A7M6
2	50S ribosomal protein L30	protein	58	36% helix, 21% strand	P0AG51
3	50S ribosomal protein L32	protein	56	9% helix, 7% strand	P0A7N4
4	50S ribosomal protein L33	protein	50	0% helix, 46% strand	P0A7N9
5	50S ribosomal protein L1	protein	234	27% helix, 21% strand	P0A7L0
6	50S ribosomal protein L34	protein	46	43% helix, 0% strand	P0A7P5
7	50S ribosomal protein L35	protein	64	20% helix, 9% strand	P0A7Q1
8	50S ribosomal protein L36	protein	38	0% helix, 16% strand	P0A7Q6
9	GTPase OBGE/CGTA	protein	333	20% helix, 18% strand	P42641
A	5S rRNA	rna	115	—	—
B	23S rRNA	rna	2903	—	—
C	50S ribosomal protein L2	protein	271	5% helix, 25% strand	P60422
D	50S ribosomal protein L3	protein	209	4% helix, 26% strand	P60438
E	50S ribosomal protein L4	protein	201	28% helix, 5% strand	P60723
F	50S ribosomal protein L5	protein	178	14% helix, 15% strand	P62399
G	50S ribosomal protein L6	protein	175	16% helix, 15% strand	P0AG55
H	50S ribosomal protein L9	protein	149	22% helix, 20% strand	P0A7R1
I	50S ribosomal protein L11	protein	69	51% helix, 12% strand	P0A7J7
J	50S ribosomal protein L13	protein	142	20% helix, 14% strand	P0AA10
K	50S ribosomal protein L14	protein	121	2% helix, 31% strand	P0ADY3
L	50S ribosomal protein L15	protein	143	10% helix, 11% strand	P02413
M	50S ribosomal protein L16	protein	136	21% helix, 23% strand	P0ADY7
N	50S ribosomal protein L17	protein	120	35% helix, 13% strand	P0AG44
O	50S ribosomal protein L18	protein	116	26% helix, 15% strand	P0C018
P	50S ribosomal protein L19	protein	114	11% helix, 14% strand	P0A7K6
Q	50S ribosomal protein L20	protein	117	57% helix, 0% strand	P0A7L3
R	50S ribosomal protein L21	protein	103	0% helix, 36% strand	P0AG48
S	50S ribosomal protein L22	protein	110	26% helix, 39% strand	P61175
T	50S ribosomal protein L23	protein	93	14% helix, 19% strand	P0ADZ0
U	50S ribosomal protein L24	protein	99	0% helix, 31% strand	P60624
W	50S ribosomal protein L25	protein	94	23% helix, 50% strand	P68919
Y	50S ribosomal protein L27	protein	79	0% helix, 3% strand	P0A7L8

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	892	0.90	0.93	86	empty
2	1139	0.88	0.90	112	empty
3	930	0.86	0.88	82	empty
4	741	0.86	0.90	64	empty
5	558	0.85	0.91	42	empty

Interfaces

63 interfaces between chains.

B–C · 7252 Å² buried · 192 hydrogen bonds · protein-nucleic
B–D · 5173 Å² buried · 128 hydrogen bonds · protein-nucleic
B–L · 4671 Å² buried · 157 hydrogen bonds · protein-nucleic
B–E · 4338 Å² buried · 105 hydrogen bonds · protein-nucleic
B–Q · 4247 Å² buried · 128 hydrogen bonds · protein-nucleic

Compared structures

4CSU · Cryo-EM structures of the 50S ribosome subunit bound with ObgE · 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 P0A7M2
Every structure of UniProt P0A7M6
Every structure of UniProt P0AG51
Every structure of UniProt P0A7N4
Every structure of UniProt P0A7N9
Every structure of UniProt P0A7L0
Every structure of UniProt P0A7P5
Every structure of UniProt P0A7Q1
Every structure of UniProt P0A7Q6
Every structure of UniProt P42641
Every structure of UniProt P60422
Every structure of UniProt P60438
Every structure of UniProt P60723
Every structure of UniProt P62399
Every structure of UniProt P0AG55
Every structure of UniProt P0A7R1
Every structure of UniProt P0A7J7
Every structure of UniProt P0AA10
Every structure of UniProt P0ADY3
Every structure of UniProt P02413
Every structure of UniProt P0ADY7
Every structure of UniProt P0AG44
Every structure of UniProt P0C018
Every structure of UniProt P0A7K6
Every structure of UniProt P0A7L3
Every structure of UniProt P0AG48
Every structure of UniProt P61175
Every structure of UniProt P0ADZ0
Every structure of UniProt P60624
Every structure of UniProt P68919
Every structure of UniProt P0A7L8
Elsewhere: RCSB PDB 4CSU · PDBe 4CSU · UniProt P0A7M2 · UniProt P0A7M6 · UniProt P0AG51 · UniProt P0A7N4 · UniProt P0A7N9 · UniProt P0A7L0 · UniProt P0A7P5 · UniProt P0A7Q1 · UniProt P0A7Q6 · UniProt P42641 · UniProt P60422 · UniProt P60438 · UniProt P60723 · UniProt P62399 · UniProt P0AG55 · UniProt P0A7R1 · UniProt P0A7J7 · UniProt P0AA10 · UniProt P0ADY3 · UniProt P02413 · UniProt P0ADY7 · UniProt P0AG44 · UniProt P0C018 · UniProt P0A7K6 · UniProt P0A7L3 · UniProt P0AG48 · UniProt P61175 · UniProt P0ADZ0 · UniProt P60624 · UniProt P68919 · UniProt P0A7L8

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