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Crystal structure of DREP2 cide domain

Analyse Crystal structure of DREP2 cide domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4D2K
Type: protein
Length: 321 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DREP2
UniProt: Q9U787
Pockets: 4 · best druggability 0.66

Structure

x-ray diffraction · 2 distinct chains · 20% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DREP2	protein	81	20% helix, 32% strand	Q9U787
B, C, D	DREP2	protein	80	21% helix, 33% strand	Q9U787

Pockets

4 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	397	0.66	0.79	56	empty
2	230	0.53	0.76	32	empty
3	70	0.32	0.75	13	empty
4	70	0.32	0.75	14	empty

Interfaces

5 interfaces between chains.

C–D · 498 Å² buried · 5 hydrogen bonds · protein-protein
A–B · 469 Å² buried · 9 hydrogen bonds · protein-protein
B–C · 386 Å² buried · 3 hydrogen bonds · protein-protein
A–C · 174 Å² buried · 4 hydrogen bonds · protein-protein
A–D · 104 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

4D2K · Crystal structure of DREP2 CIDE domain · 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 Q9U787
Elsewhere: RCSB PDB 4D2K · PDBe 4D2K · UniProt Q9U787

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