Research workbench

SAC3:SUS1:CDC31:NUP1 complex

Analyse SAC3:SUS1:CDC31:NUP1 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4MBE
Type: protein
Length: 610 residues
Chains: 10
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cell division control protein 31; Nuclear mRNA export protein SAC3; Protein SUS1…
UniProt: P06704, P46674, Q6WNK7, P20676
Ligands: CA
Pockets: 8 · best druggability 0.75

Structure

x-ray diffraction · 9 distinct chains · 69% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, D	Cell division control protein 31	protein	149	58% helix, 5% strand	P06704
B	Nuclear mRNA export protein SAC3	protein	50	96% helix, 0% strand	P46674
C	Protein SUS1	protein	94	72% helix, 1% strand	Q6WNK7
E	Nuclear mRNA export protein SAC3	protein	51	96% helix, 0% strand	P46674
F	Protein SUS1	protein	88	76% helix, 0% strand	Q6WNK7
H	Nucleoporin NUP1	protein	10	0% helix, 0% strand	P20676
G	Nucleoporin NUP1	protein	9	0% helix, 0% strand	P20676
X	Nucleoporin NUP1	protein	6	0% helix, 17% strand	P20676
Y	Nucleoporin NUP1	protein	4	0% helix, 0% strand	P20676

Ligands and binding sites

CA · Calcium ion · metal · 4 copies · chains A, D

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	921	0.75	0.79	88	empty
2	306	0.57	0.76	40	empty
3	235	0.52	0.76	29	empty
4	155	0.50	0.78	22	empty
5	152	0.48	0.77	28	empty

Interfaces

22 interfaces between chains.

B–C · 1595 Å² buried · 12 hydrogen bonds · protein-protein
E–F · 1570 Å² buried · 10 hydrogen bonds · protein-protein
D–E · 1460 Å² buried · 13 hydrogen bonds · protein-protein
A–B · 1427 Å² buried · 10 hydrogen bonds · protein-protein
C–G · 385 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

4MBE · Sac3:Sus1:Cdc31:Nup1 complex · the same entry in another collection · chain Y against Y, TM-score 1.00
P20676 · AlphaFold monomer V2.0 prediction for nucleoporin NUP1 (P20676) · a predicted model of the same protein · chain Y against A, TM-score 0.99
P06704 · AlphaFold monomer V2.0 prediction for cell division control protein 31 (P06704) · a predicted model of the same protein · chain A against A, TM-score 0.89

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 P06704
Every structure of UniProt P46674
Every structure of UniProt Q6WNK7
Every structure of UniProt P20676
Elsewhere: RCSB PDB 4MBE · PDBe 4MBE · UniProt P06704 · UniProt P46674 · UniProt Q6WNK7 · UniProt P20676

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