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Cryo-EM structure of the human mtLSU assembly intermediate upon MRM2 depletion - class 4

Analyse Cryo-EM structure of the human mtLSU assembly intermediate upon MRM2 depletion… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7QH7
Type
protein + RNA
Length
8,329 residues
Chains
49
Method
electron microscopy
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.89
Source
Homo sapiens
Molecule
39S ribosomal protein L2, mitochondrial; 39S ribosomal protein L3, mitochondrial; 39S…
EC
3.1.26.-
UniProt
Q5T653, P09001, Q9BYD3, Q9BYD2, Q7Z7H8, Q9BYD1, Q6P1L8, Q9P015, Q9NX20, Q9NRX2, Q9H0U6, P49406, Q9BYC9, Q7Z2W9, Q9NWU5, Q96A35, Q9P0M9, Q13084, Q9HD33, Q8TCC3, Q9BYC8, O75394, Q9BQ48, Q9NZE8, Q9BZE1, Q9NYK5, Q8IXM3, Q8N983, Q9H9J2, Q9BRJ2, Q13405, Q8N5N7, Q4U2R6, Q86TS9, Q9BQC6, Q8TAE8, Q9NVS2, Q9NP92, Q96EH3, L0R8F8, O14561, Q9P0J6
Ligands
MG, ZN
Pockets
20 · best druggability 0.88

Structure

electron microscopy · resolution 2.89 · 49 distinct chains · 31% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
D39S ribosomal protein L2, mitochondrialprotein2155% helix, 28% strandQ5T653
E39S ribosomal protein L3, mitochondrialprotein30414% helix, 26% strandP09001
F39S ribosomal protein L4, mitochondrialprotein25030% helix, 15% strandQ9BYD3
H39S ribosomal protein L9, mitochondrialprotein9525% helix, 29% strandQ9BYD2
I39S ribosomal protein L10, mitochondrialprotein3040% helix, 0% strandQ7Z7H8
K39S ribosomal protein L13, mitochondrialprotein17738% helix, 16% strandQ9BYD1
L39S ribosomal protein L14, mitochondrialprotein1155% helix, 29% strandQ6P1L8
M39S ribosomal protein L15, mitochondrialprotein28731% helix, 11% strandQ9P015
N39S ribosomal protein L16, mitochondrialprotein20128% helix, 20% strandQ9NX20
O39S ribosomal protein L17, mitochondrialprotein15249% helix, 10% strandQ9NRX2
P39S ribosomal protein L18, mitochondrialprotein14133% helix, 17% strandQ9H0U6
Q39S ribosomal protein L19, mitochondrialprotein21724% helix, 22% strandP49406
R39S ribosomal protein L20, mitochondrialprotein13969% helix, 0% strandQ9BYC9
S39S ribosomal protein L21, mitochondrialprotein15613% helix, 42% strandQ7Z2W9
T39S ribosomal protein L22, mitochondrialprotein15534% helix, 19% strandQ9NWU5
U39S ribosomal protein L23, mitochondrialprotein12510% helix, 21% strand—
V39S ribosomal protein L24, mitochondrialprotein4825% helix, 6% strandQ96A35
W39S ribosomal protein L27, mitochondrialprotein1000% helix, 40% strandQ9P0M9
X39S ribosomal protein L28, mitochondrialprotein24345% helix, 15% strandQ13084
Y39S ribosomal protein L47, mitochondrialprotein17558% helix, 7% strandQ9HD33
Z39S ribosomal protein L30, mitochondrialprotein11520% helix, 20% strandQ8TCC3
039S ribosomal protein L32, mitochondrialprotein10831% helix, 13% strandQ9BYC8
139S ribosomal protein L33, mitochondrialprotein490% helix, 59% strandO75394
239S ribosomal protein L34, mitochondrialprotein4553% helix, 0% strandQ9BQ48
339S ribosomal protein L35, mitochondrialprotein9527% helix, 8% strandQ9NZE8
539S ribosomal protein L37, mitochondrialprotein39225% helix, 24% strandQ9BZE1
639S ribosomal protein L38, mitochondrialprotein29223% helix, 19% strand—
739S ribosomal protein L39, mitochondrialprotein28733% helix, 24% strandQ9NYK5
939S ribosomal protein L41, mitochondrialprotein11726% helix, 9% strandQ8IXM3
a39S ribosomal protein L42, mitochondrialprotein8025% helix, 14% strand—
b39S ribosomal protein L43, mitochondrialprotein14821% helix, 19% strandQ8N983
c39S ribosomal protein L44, mitochondrial (EC 3.1.26.-)protein27556% helix, 8% strandQ9H9J2
d39S ribosomal protein L45, mitochondrialprotein15725% helix, 28% strandQ9BRJ2
f39S ribosomal protein L48, mitochondrialprotein1718% helix, 0% strand—
g39S ribosomal protein L49, mitochondrialprotein12923% helix, 24% strandQ13405
h39S ribosomal protein L50, mitochondrialprotein10144% helix, 8% strandQ8N5N7
i39S ribosomal protein L51, mitochondrialprotein9744% helix, 1% strandQ4U2R6
j39S ribosomal protein L52, mitochondrialprotein8660% helix, 5% strandQ86TS9
oRibosomal protein 63, mitochondrialprotein8160% helix, 1% strandQ9BQC6
pPeptidyl-tRNA hydrolase ICT1, mitochondrialprotein12534% helix, 15% strand—
qGrowth arrest and DNA damage-inducible proteins-interacting protein 1protein10160% helix, 1% strandQ8TAE8
r39S ribosomal protein S18a, mitochondrialprotein12923% helix, 5% strandQ9NVS2
s39S ribosomal protein S30, mitochondrialprotein37029% helix, 18% strandQ9NP92
uMitochondrial assembly of ribosomal large subunit protein 1protein11136% helix, 21% strandQ96EH3
vMIEF1 upstream open reading frame proteinprotein6958% helix, 3% strandL0R8F8
wAcyl carrier protein, mitochondrialprotein7951% helix, 0% strandO14561
A16S ribosomal RNArna1256——
Bmitochondrial tRNAValrna56——
439S ribosomal protein L36, mitochondrialprotein378% helix, 43% strandQ9P0J6

Ligands and binding sites

  • MG · Magnesium ion · metal · 50 copies · chains E, A, F, Q, s, M, U, R
  • ZN · Zinc ion · metal · 3 copies · chains 0, I, r, 4

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
17790.880.9294empty
29010.870.9090MG
39360.860.8878empty
47010.850.8977empty
58580.830.8689empty

Interfaces

173 interfaces between chains.

  • E–A · 5047 Ų buried · 91 hydrogen bonds · protein-nucleic
  • M–A · 4079 Ų buried · 82 hydrogen bonds · protein-nucleic
  • D–A · 3760 Ų buried · 88 hydrogen bonds · protein-nucleic
  • F–A · 3609 Ų buried · 67 hydrogen bonds · protein-nucleic
  • R–A · 3163 Ų buried · 62 hydrogen bonds · protein-nucleic

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 7QH7 · Cryo-EM structure of the human mtlsu assembly intermediate upon MRM2 depletion - class 4 · the same entry in another collection · chain B against B, TM-score 1.00

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