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DREP3

Analyse DREP3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7V6E
Type: protein
Length: 693 residues
Chains: 9
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dnaation factor-related protein 3, isoform a
UniProt: Q0E9B7
Pockets: 9 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 23% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I	Dnaation factor-related protein 3, isoform a	protein	77	23% helix, 30% strand	Q0E9B7

Pockets

9 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	278	0.59	0.78	41	empty
2	207	0.54	0.78	35	empty
3	167	0.50	0.77	31	empty
4	87	0.47	0.81	17	empty
5	96	0.35	0.74	18	empty

Interfaces

12 interfaces between chains.

G–H · 530 Å² buried · 6 hydrogen bonds · protein-protein
B–C · 508 Å² buried · 7 hydrogen bonds · protein-protein
A–G · 497 Å² buried · 10 hydrogen bonds · protein-protein
C–I · 497 Å² buried · 6 hydrogen bonds · protein-protein
D–F · 495 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

7V6E · DREP3 · the same entry in another collection · chain A against A, TM-score 1.00

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 Q0E9B7
Elsewhere: RCSB PDB 7V6E · PDBe 7V6E · UniProt Q0E9B7

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