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A heterospecific leucine zipper tetramer

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

PDB: 3CK4
Type: protein
Length: 387 residues
Chains: 12
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: GCN4 leucine zipper
UniProt: P03069
Ligands: MG
Pockets: 4 · best druggability 0.78

Structure

x-ray diffraction · 8 distinct chains · 90% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, I, L	GCN4 leucine zipper	protein	31	94% helix, 0% strand	P03069
B	GCN4 leucine zipper	protein	32	91% helix, 0% strand	P03069
C, F, J	GCN4 leucine zipper	protein	34	88% helix, 0% strand	P03069
D	GCN4 leucine zipper	protein	33	94% helix, 0% strand	P03069
E	GCN4 leucine zipper	protein	31	90% helix, 0% strand	P03069
G	GCN4 leucine zipper	protein	33	91% helix, 0% strand	P03069
H	GCN4 leucine zipper	protein	30	87% helix, 0% strand	P03069
K	GCN4 leucine zipper	protein	33	88% helix, 0% strand	P03069

Ligands and binding sites

MG · Magnesium ion · metal · 4 copies · chains B, C, F, G, I, J, K

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1161	0.78	0.79	70	empty
2	99	0.41	0.77	24	empty
3	98	0.35	0.74	17	empty
4	64	0.29	0.74	12	empty

Interfaces

26 interfaces between chains.

C–D · 896 Å² buried · 5 hydrogen bonds · protein-protein
F–G · 886 Å² buried · 6 hydrogen bonds · protein-protein
B–C · 867 Å² buried · 8 hydrogen bonds · protein-protein
I–J · 857 Å² buried · 6 hydrogen bonds · protein-protein
K–L · 837 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

3CK4 · A heterospecific leucine zipper tetramer · the same entry in another collection · chain L against L, 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 P03069
Elsewhere: RCSB PDB 3CK4 · PDBe 3CK4 · UniProt P03069

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