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Structure of a BRCA2-DSS1 complex

Analyse Structure of a BRCA2-DSS1 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1IYJ
Type: protein
Length: 1,272 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Deleted in split HAND/SPLIT foot protein 1; Breast cancer susceptibility
UniProt: P60896, O35923
Pockets: 18 · best druggability 0.82

Structure

x-ray diffraction · 2 distinct chains · 26% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Deleted in split HAND/SPLIT foot protein 1	protein	45	16% helix, 2% strand	P60896
B, D	Breast cancer susceptibility	protein	591	26% helix, 20% strand	O35923

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1174	0.82	0.83	113	empty
2	158	0.51	0.79	22	empty
3	151	0.48	0.78	22	empty
4	157	0.46	0.76	20	empty
5	210	0.45	0.74	30	empty

Interfaces

3 interfaces between chains.

C–D · 2887 Å² buried · 44 hydrogen bonds · protein-protein
A–B · 2877 Å² buried · 43 hydrogen bonds · protein-protein
B–D · 761 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

1IYJ · Structure of a BRCA2-DSS1 complex · the same entry in another collection · chain A against A, TM-score 1.00
P60896 · AlphaFold monomer V2.0 prediction for 26S proteasome complex subunit SEM1 (P60896) · a predicted model of the same protein · chain A against A, TM-score 0.22

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 P60896
Every structure of UniProt O35923
Elsewhere: RCSB PDB 1IYJ · PDBe 1IYJ · UniProt P60896 · UniProt O35923

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