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Cryo-EM structure of yeast ribonuclease mrp with substrate ITS1

Analyse Cryo-EM structure of yeast ribonuclease mrp with substrate ITS1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7C7A
Type
protein + RNA
Length
2,858 residues
Chains
13
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ribonuclease mrp RNA subunit NME1; Ribonucleases P/MRP protein subunit POP1…
EC
3.1.26.5
UniProt
P41812, P53833, P38336, P28005, P53218, P38291, P38208, P38786, P40993, Q12530
Ligands
MG, ZN
Pockets
20 · best druggability 0.84

Structure

electron microscopy · 13 distinct chains · 39% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARibonuclease mrp RNA subunit NME1rna330——
BRibonucleases P/MRP protein subunit POP1 (EC 3.1.26.5)protein79335% helix, 17% strandP41812
CRibonucleases P/MRP protein subunit POP3protein15234% helix, 14% strandP53833
DRnases MRP/P 32.9 kda subunitprotein25145% helix, 17% strandP38336
ERibonuclease P/MRP protein subunit POP5 (EC 3.1.26.5)protein14541% helix, 21% strandP28005
FRibonucleases P/MRP protein subunit POP6 (EC 3.1.26.5)protein15725% helix, 34% strandP53218
GRibonucleases P/MRP protein subunit POP7 (EC 3.1.26.5)protein12128% helix, 35% strandP38291
HRibonucleases P/MRP protein subunit POP8 (EC 3.1.26.5)protein13141% helix, 21% strandP38208
IRibonuclease P/MRP protein subunit RPP1 (EC 3.1.26.5)protein24243% helix, 18% strandP38786
JRibonuclease P/MRP protein subunit RPP1 (EC 3.1.26.5)protein29237% helix, 15% strandP38786
KRibonuclease mrp protein subunit SNM1protein10442% helix, 11% strandP40993
LRibonuclease mrp protein subunit RMP1protein13178% helix, 0% strandQ12530
RInternal transcribed spacer 1rna9——

Ligands and binding sites

  • MG · Magnesium ion · metal · 3 copies · chains A, R
  • ZN · Zinc ion · metal · chains K

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
19610.840.8677MG
27960.820.8660empty
33280.820.9242empty
44320.820.9162empty
511430.820.8379empty

Interfaces

33 interfaces between chains.

  • A–B · 8213 Ų buried · 142 hydrogen bonds · protein-nucleic
  • D–J · 2402 Ų buried · 23 hydrogen bonds · protein-protein
  • A–D · 2042 Ų buried · 28 hydrogen bonds · protein-nucleic
  • B–L · 1927 Ų buried · 13 hydrogen bonds · protein-protein
  • A–G · 1873 Ų buried · 29 hydrogen bonds · protein-nucleic

Compared structures

  • 7C7A · Cryo-EM structure of yeast Ribonuclease MRP with substrate ITS1 · the same entry in another collection · chain R against R, TM-score 1.00

Analyse

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