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Ribosome nascent chain in complex with seca

Analyse Ribosome nascent chain in complex with seca in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6S0K
Type
protein + RNA
Length
7,390 residues
Chains
35
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
TRNA-cca; 23S ribosomal RNA; 5S ribosomal RNA; 50S ribosomal protein L2; 50S ribosomal…
UniProt
P60422, P60438, P60723, P62399, P0AG55, P0A7R1, A0A073UC57, P0A7J7, P0AA10, P0ADY3, P02413, P0ADY7, P0AG44, P0C018, P0A7K6, P0A7L3, P0AG48, P61175, P0ADZ0, P60624, P68919, P0A7L8, P0A7M2, P0A7M6, P0AG51, P0A7N4, P0A7N9, P0A7P5, P0A7Q1, P0A7Q6, A0A037YQ84
Ligands
MG, ZN
Pockets
20 · best druggability 0.87

Structure

electron microscopy · 35 distinct chains · 31% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
2TRNA-ccarna3——
A23S ribosomal RNArna2883——
B5S ribosomal RNArna120——
C50S ribosomal protein L2protein2715% helix, 30% strandP60422
D50S ribosomal protein L3protein2099% helix, 38% strandP60438
E50S ribosomal protein L4protein20132% helix, 13% strandP60723
F50S ribosomal protein L5protein17738% helix, 21% strandP62399
G50S ribosomal protein L6protein17618% helix, 37% strandP0AG55
H50S ribosomal protein L9protein14932% helix, 26% strandP0A7R1
I50S ribosomal protein L10protein12550% helix, 17% strandA0A073UC57
J50S ribosomal protein L11protein13437% helix, 16% strandP0A7J7
K50S ribosomal protein L13protein14234% helix, 21% strandP0AA10
L50S ribosomal protein L14protein1237% helix, 38% strandP0ADY3
M50S ribosomal protein L15protein14417% helix, 14% strandP02413
N50S ribosomal protein L16protein13619% helix, 28% strandP0ADY7
O50S ribosomal protein L17protein12554% helix, 16% strandP0AG44
P50S ribosomal protein L18protein11744% helix, 20% strandP0C018
Q50S ribosomal protein L19protein11415% helix, 45% strandP0A7K6
R50S ribosomal protein L20protein11779% helix, 0% strandP0A7L3
S50S ribosomal protein L21protein1030% helix, 65% strandP0AG48
T50S ribosomal protein L22protein11035% helix, 35% strandP61175
U50S ribosomal protein L23protein9227% helix, 38% strandP0ADZ0
V50S ribosomal protein L24protein1026% helix, 49% strandP60624
W50S ribosomal protein L25protein9421% helix, 47% strandP68919
X50S ribosomal protein L27protein760% helix, 42% strandP0A7L8
Y50S ribosomal protein L28protein7727% helix, 36% strandP0A7M2
Z50S ribosomal protein L29protein6271% helix, 0% strandP0A7M6
a50S ribosomal protein L30protein5831% helix, 26% strandP0AG51
b50S ribosomal protein L32protein5618% helix, 18% strandP0A7N4
c50S ribosomal protein L33protein510% helix, 55% strandP0A7N9
d50S ribosomal protein L34protein4652% helix, 0% strandP0A7P5
e50S ribosomal protein L35protein6431% helix, 13% strandP0A7Q1
f50S ribosomal protein L36protein388% helix, 47% strandP0A7Q6
hProtein translocase subunit secaprotein83849% helix, 9% strandA0A037YQ84
kCytoskeleton protein rodzprotein5730% helix, 0% strand—

Ligands and binding sites

  • MG · Magnesium ion · metal · 68 copies · chains A, D, C, e, M, O, U, B, b
  • ZN · Zinc ion · metal · chains f

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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111180.870.89110empty
28570.870.9182MG
310600.870.8990empty
47130.860.9186MG
56200.860.9252MG

Interfaces

73 interfaces between chains.

  • A–C · 7110 Ų buried · 170 hydrogen bonds · protein-nucleic
  • A–D · 5056 Ų buried · 108 hydrogen bonds · protein-nucleic
  • A–M · 4582 Ų buried · 115 hydrogen bonds · protein-nucleic
  • A–E · 4265 Ų buried · 96 hydrogen bonds · protein-nucleic
  • A–R · 4177 Ų buried · 102 hydrogen bonds · protein-nucleic

Compared structures

  • 6S0K · Ribosome nascent chain in complex with SecA · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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