Research workbench

GCN4-P1 peptide trimer with tyrosine residue at position 16

Analyse GCN4-P1 peptide trimer with tyrosine residue at position 16 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6XNM
Type: protein
Length: 90 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: GCN4-P1 peptide with A16; GCN4-P1 peptide with Y16
UniProt: P03069
Ligands: NA

Structure

x-ray diffraction · 2 distinct chains · 92% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	GCN4-P1 peptide with A16	protein	30	93% helix, 0% strand	P03069
B	GCN4-P1 peptide with Y16	protein	30	90% helix, 0% strand	P03069

Ligands and binding sites

NA · Sodium ion · metal · 7 copies · chains A, C, B

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

Interfaces

3 interfaces between chains.

B–C · 736 Å² buried · 3 hydrogen bonds · protein-protein
A–B · 662 Å² buried · 2 hydrogen bonds · protein-protein
A–C · 661 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

6XNM · GCN4-p1 Peptide Trimer with tyrosine residue at position 16 · the same entry in another collection · chain A against A, 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 B against A, TM-score 0.90

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 6XNM · PDBe 6XNM · UniProt P03069

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