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Coiled-coil structure of liprin-ALPHA2_H2DELC

Analyse Coiled-coil structure of liprin-ALPHA2_H2DELC in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7D2G
Type: protein
Length: 198 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Liprin-alpha-2
UniProt: O75334
Pockets: 3 · best druggability 0.47

Structure

x-ray diffraction · 3 distinct chains · 94% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Liprin-alpha-2	protein	51	90% helix, 0% strand	O75334
B, D	Liprin-alpha-2	protein	50	96% helix, 0% strand	O75334
C	Liprin-alpha-2	protein	47	96% helix, 0% strand	O75334

Ligands and binding sites

GOL · Glycerol · additive · chains C, D

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

Pockets

3 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	154	0.47	0.76	17	empty
2	93	0.44	0.79	16	empty
3	76	0.38	0.77	15	empty

Interfaces

5 interfaces between chains.

C–D · 1153 Å² buried · 9 hydrogen bonds · protein-protein
A–B · 1138 Å² buried · 8 hydrogen bonds · protein-protein
A–C · 770 Å² buried · 11 hydrogen bonds · protein-protein
A–D · 210 Å² buried · 3 hydrogen bonds · protein-protein
B–C · 195 Å² buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified, 2 disulfide (engineered, disulfide).

Compared structures

7D2G · Coiled-coil structure of liprin-alpha2_H2delC · the same entry in another collection · chain A against A, TM-score 1.00
O75334 · AlphaFold monomer V2.0 prediction for liprin-alpha-2 (O75334) · a predicted model of the same protein · chain C against A, TM-score 0.94

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 O75334
Elsewhere: RCSB PDB 7D2G · PDBe 7D2G · UniProt O75334

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