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The cryo-EM structure of the human 17S U2 snrnp

Analyse The cryo-EM structure of the human 17S U2 snrnp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7EVO
Type
protein + RNA
Length
4,817 residues
Chains
21
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
U2 snrna; Splicing factor 3B subunit 1; Splicing factor 3B subunit 2; Splicing factor 3B…
EC
3.6.4.13
UniProt
O75533, Q13435, Q15393, Q15427, Q9BWJ5, Q7RTV0, Q15459, Q15428, Q12874, O43719, A0A0C4DG89, P09661, P08579, P62316, P62306, P62304, P62308, P62318, P14678, P62314
Ligands
9B0, ZN
Pockets
20 · best druggability 0.84

Structure

electron microscopy · 21 distinct chains · 33% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
HU2 snrnarna148——
1Splicing factor 3B subunit 1protein81576% helix, 0% strandO75533
2Splicing factor 3B subunit 2protein18227% helix, 5% strandQ13435
3Splicing factor 3B subunit 3protein11807% helix, 46% strandQ15393
4Splicing factor 3B subunit 4protein16023% helix, 29% strandQ15427
5Splicing factor 3B subunit 5protein6661% helix, 0% strandQ9BWJ5
6Phd finger-like domain-containing protein 5Aprotein8513% helix, 25% strandQ7RTV0
ASplicing factor 3A subunit 1protein12359% helix, 0% strandQ15459
BSplicing factor 3A subunit 2protein1004% helix, 33% strandQ15428
CSplicing factor 3A subunit 3protein42255% helix, 3% strandQ12874
DHIV tat-specific factor 1protein20028% helix, 26% strandO43719
ERNA helicase (EC 3.6.4.13)protein45543% helix, 13% strandA0A0C4DG89
FU2 small nuclear ribonucleoprotein a'protein16223% helix, 17% strandP09661
GU2 small nuclear ribonucleoprotein B''protein16628% helix, 27% strandP08579
aSmall nuclear ribonucleoprotein sm D2protein9018% helix, 49% strandP62316
bSmall nuclear ribonucleoprotein Fprotein749% helix, 58% strandP62306
cSmall nuclear ribonucleoprotein Eprotein7914% helix, 53% strandP62304
dSmall nuclear ribonucleoprotein Gprotein740% helix, 50% strandP62308
eSmall nuclear ribonucleoprotein sm D3protein8310% helix, 43% strandP62318
fSmall nuclear ribonucleoprotein-associated proteins B and B'protein714% helix, 52% strandP14678
gSmall nuclear ribonucleoprotein sm D1protein8212% helix, 46% strandP62314

Ligands and binding sites

  • 9B0 · [(2~{S},3~{S},4~{E},6~{S},7~{R},10~{R})-3,7-dimethyl-2-[(2~{E},4~{E},6~{R})-6-methyl-6-oxidanyl-7-[(2~{R}, 3~{R})-3-[(2~{R},3~{S})-3-oxidanylpentan-2-yl]oxiran-2-yl]hepta-2,4-dien-2-yl]-7,10-bis(oxidanyl)-12-oxidanylidene-1-oxacyclododec-4-en-6-yl] 4-cycloheptylpiperazine-1-carboxylate · ligand · chains 1, 6
  • ZN · Zinc ion · metal · 4 copies · chains 6, C

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
110670.840.85101empty
211540.840.8578empty
36810.790.8489empty
410770.780.8069empty
52750.770.9055empty

Interfaces

39 interfaces between chains.

  • 3–5 · 2333 Ų buried · 26 hydrogen bonds · protein-protein
  • 1–2 · 2284 Ų buried · 14 hydrogen bonds · protein-protein
  • 1–3 · 2178 Ų buried · 20 hydrogen bonds · protein-protein
  • 1–E · 1910 Ų buried · 16 hydrogen bonds · protein-protein
  • 1–5 · 1454 Ų buried · 14 hydrogen bonds · protein-protein

Compared structures

  • 7EVO · The cryo-EM structure of the human 17S U2 snRNP · the same entry in another collection · chain D against D, TM-score 1.00

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