Research workbench

SGF11:SUS1 complex

Analyse SGF11:SUS1 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3KJL
Type: protein
Length: 450 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein SUS1; Saga-associated factor 11
UniProt: Q6WNK7, Q03067
Pockets: 3 · best druggability 0.79

Structure

x-ray diffraction · 7 distinct chains · 80% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein SUS1	protein	86	86% helix, 0% strand	Q6WNK7
E, H	Saga-associated factor 11	protein	32	81% helix, 0% strand	Q03067
B	Protein SUS1	protein	83	76% helix, 0% strand	Q6WNK7
F	Saga-associated factor 11	protein	28	79% helix, 0% strand	Q03067
C	Protein SUS1	protein	79	77% helix, 0% strand	Q6WNK7
G	Saga-associated factor 11	protein	23	87% helix, 0% strand	Q03067
D	Protein SUS1	protein	87	78% helix, 0% strand	Q6WNK7

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1047	0.79	0.80	82	empty
2	71	0.48	0.83	15	empty
3	55	0.26	0.73	13	empty

Interfaces

20 interfaces between chains.

D–H · 1124 Å² buried · 3 hydrogen bonds · protein-protein
B–F · 1119 Å² buried · 5 hydrogen bonds · protein-protein
A–E · 1094 Å² buried · 2 hydrogen bonds · protein-protein
C–G · 1040 Å² buried · 5 hydrogen bonds · protein-protein
A–D · 414 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

3KJL · Sgf11:Sus1 complex · the same entry in another collection · chain H against H, TM-score 1.00
Q6WNK7 · AlphaFold monomer V2.0 prediction for transcription and mRNA export factor SUS1 (Q6WNK7) · a predicted model of the same protein · chain C against A, TM-score 0.84

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 Q6WNK7
Every structure of UniProt Q03067
Elsewhere: RCSB PDB 3KJL · PDBe 3KJL · UniProt Q6WNK7 · UniProt Q03067

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