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APC10/DOC1 subunit of S. cerevisiae

Analyse APC10/DOC1 subunit of S. cerevisiae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1GQP
Type: protein
Length: 368 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DOC1/APC10
UniProt: P53068
Ligands: BR
Pockets: 6 · best druggability 0.49

Structure

x-ray diffraction · 2 distinct chains · 17% helix, 43% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DOC1/APC10	protein	180	18% helix, 45% strand	P53068
B	DOC1/APC10	protein	188	16% helix, 42% strand	P53068

Ligands and binding sites

BR · Bromide ion · ion · 6 copies · chains A, B

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

Pockets

6 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	65	0.49	0.85	25	empty
2	142	0.48	0.78	22	empty
3	64	0.42	0.81	15	empty
4	56	0.41	0.81	17	empty
5	76	0.32	0.75	16	empty

Interfaces

1 interface between chains.

A–B · 749 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

1GQP · APC10/DOC1 SUBUNIT OF S. cerevisiae · the same entry in another collection · chain A against A, TM-score 1.00
P53068 · AlphaFold monomer V2.0 prediction for anaphase-promoting complex subunit DOC1 (P53068) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P53068
Elsewhere: RCSB PDB 1GQP · PDBe 1GQP · UniProt P53068

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