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Human pre-bact-2 spliceosome core structure

Analyse Human pre-bact-2 spliceosome core structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7AAV
Type
protein + RNA
Length
4,151 residues
Chains
17
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
116 kda U5 small nuclear ribonucleoprotein component; Protein BUD31 homolog; Cell…
UniProt
Q15029, P41223, Q99459, Q9P013, P55081, O43660, O60508, Q8NAV1, Q6P2Q9, Q9NW64, Q13573, Q96NC0, Q9BZL1
Ligands
GTP, KGN, MG
Pockets
20 · best druggability 0.89

Structure

electron microscopy · 17 distinct chains · 33% helix, 11% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
r116 kda U5 small nuclear ribonucleoprotein componentprotein89527% helix, 14% strandQ15029
QProtein BUD31 homologprotein13838% helix, 0% strandP41223
LCell division cycle 5-like proteinprotein10360% helix, 0% strandQ99459
RSpliceosome-associated protein CWC15 homologprotein4414% helix, 2% strandQ9P013
KMicrofibrillar-associated protein 1protein12334% helix, 0% strandP55081
GPleiotropic regulator 1protein3200% helix, 38% strandO43660
ZMinx M3 pre-mRNArna29——
8Pre-mRNA-processing factor 17protein1850% helix, 6% strandO60508
IPre-mRNA-splicing factor 38Aprotein17647% helix, 9% strandQ8NAV1
APre-mRNA-processing-splicing factor 8protein165642% helix, 7% strandQ6P2Q9
PPre-mRNA-splicing factor RBM22protein16220% helix, 14% strandQ9NW64
vSnw domain-containing protein 1protein20635% helix, 4% strandQ13573
NZinc finger matrin-type protein 2protein5638% helix, 0% strandQ96NC0
2U2 snrnarna10——
5U5 snrnarna69——
6U6 snrnarna73——
qUbiquitin-like protein 5protein7321% helix, 33% strandQ9BZL1

Ligands and binding sites

  • GTP · Guanosine-5'-triphosphate · ligand · chains r
  • KGN · D-chiro inositol hexakisphosphate · ligand · chains K, Z, A
  • MG · Magnesium ion · metal · chains r

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
110520.890.91166empty
29850.880.89122empty
37150.860.90100empty
46570.840.8992empty
59840.840.8583empty

Interfaces

47 interfaces between chains.

  • r–A · 2807 Ų buried · 11 hydrogen bonds · protein-protein
  • A–5 · 1902 Ų buried · 15 hydrogen bonds · protein-nucleic
  • A–v · 1827 Ų buried · 7 hydrogen bonds · protein-protein
  • K–A · 1068 Ų buried · 6 hydrogen bonds · protein-protein
  • A–q · 1049 Ų buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

  • 7AAV · Human pre-Bact-2 spliceosome core structure · the same entry in another collection · chain P against P, TM-score 1.00

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