MolNFT v1 · #60440 · protein

A heterospecific leucine zipper tetramer

3CRP · GCN4 leucine zipper: “A heterospecific leucine zipper tetramer”. X-ray diffraction, 1 ligand (NA), 1 pocket (best druggability 0.28). MolNFT v1 #60440 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3CRP
Type: protein
Length: 158 residues
Chains: 5
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: GCN4 leucine zipper
UniProt: P03069
Ligands: NA
Pockets: 1 · best druggability 0.28

Structure

x-ray diffraction · 4 distinct chains · 90% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, D	GCN4 leucine zipper	protein	32	84% helix, 0% strand	P03069
B	GCN4 leucine zipper	protein	34	88% helix, 0% strand	P03069
C	GCN4 leucine zipper	protein	31	94% helix, 0% strand	P03069
E	GCN4 leucine zipper	protein	29	93% helix, 0% strand	P03069

Ligands and binding sites

NA · Sodium ion · metal · chains B, C

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	60	0.28	0.74	12	empty

Interfaces

8 interfaces between chains.

A–B · 852 Å² buried · 5 hydrogen bonds · protein-protein
C–D · 837 Å² buried · 3 hydrogen bonds · protein-protein
B–C · 826 Å² buried · 5 hydrogen bonds · protein-protein
A–D · 525 Å² buried · 3 hydrogen bonds · protein-protein
B–E · 247 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

3CRP · A heterospecific leucine zipper tetramer · the same entry in another collection · chain E against E, TM-score 1.00
P03069 · AlphaFold monomer V2.0 prediction for general control transcription factor GCN4 (P03069) · a predicted model of the same protein · chain D against A, TM-score 0.92

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 3CRP · PDBe 3CRP · UniProt P03069

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