Research workbench

U2AF65 uhm bound to SF3B155 ULM5

Analyse U2AF65 uhm bound to SF3B155 ULM5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7SN6
Type: protein
Length: 230 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Splicing factor U2AF 65 kda subunit; Splicing factor 3B subunit 1
UniProt: P26368, O75533
Pockets: 2 · best druggability 0.41

Structure

x-ray diffraction · 4 distinct chains · 32% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Splicing factor U2AF 65 kda subunit	protein	104	35% helix, 23% strand	P26368
B	Splicing factor U2AF 65 kda subunit	protein	105	33% helix, 24% strand	P26368
C	Splicing factor 3B subunit 1	protein	12	25% helix, 8% strand	O75533
D	Splicing factor 3B subunit 1	protein	9	0% helix, 11% strand	O75533

Ligands and binding sites

IPA · Isopropyl alcohol · additive · chains B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	78	0.41	0.79	20	empty
2	135	0.41	0.74	23	empty

Interfaces

4 interfaces between chains.

A–C · 565 Å² buried · 11 hydrogen bonds · protein-protein
B–D · 516 Å² buried · 14 hydrogen bonds · protein-protein
A–B · 451 Å² buried · 5 hydrogen bonds · protein-protein
B–C · 85 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

7SN6 · U2AF65 uhm bound to SF3B155 ULM5 · the same entry in another collection · chain A against A, TM-score 1.00
P26368 · AlphaFold monomer V2.0 prediction for splicing factor U2AF 65 kda subunit (P26368) · a predicted model of the same protein · chain A against A, TM-score 0.96

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P26368
Every structure of UniProt O75533
Elsewhere: RCSB PDB 7SN6 · PDBe 7SN6 · UniProt P26368 · UniProt O75533

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