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Crystal structure of soluble form of CLIC4

Analyse Crystal structure of soluble form of CLIC4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2D2Z
Type: protein
Length: 694 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chloride intracellular channel protein 4
UniProt: Q9Y696
Pockets: 7 · best druggability 0.73

Structure

x-ray diffraction · 3 distinct chains · 45% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Chloride intracellular channel protein 4	protein	223	48% helix, 9% strand	Q9Y696
B	Chloride intracellular channel protein 4	protein	240	43% helix, 8% strand	Q9Y696
C	Chloride intracellular channel protein 4	protein	231	46% helix, 9% strand	Q9Y696

Pockets

7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	449	0.73	0.83	41	empty
2	183	0.66	0.85	22	empty
3	196	0.64	0.84	27	empty
4	184	0.60	0.82	24	empty
5	50	0.46	0.85	13	empty

Interfaces

3 interfaces between chains.

B–C · 1104 Å² buried · 19 hydrogen bonds · protein-protein
A–B · 845 Å² buried · 7 hydrogen bonds · protein-protein
A–C · 403 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

2D2Z · Crystal structure of Soluble Form Of CLIC4 · the same entry in another collection · chain A against A, TM-score 1.00
Q9Y696 · AlphaFold monomer V2.0 prediction for chloride intracellular channel protein 4 (Q9Y696) · a predicted model of the same protein · chain A against A, TM-score 0.98

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q9Y696
Elsewhere: RCSB PDB 2D2Z · PDBe 2D2Z · UniProt Q9Y696

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