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MAX1 peptide fibril

Analyse MAX1 peptide fibril in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2N1E
Type: protein
Length: 160 residues
Chains: 8
Method: solid-state nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: MAX1 peptide
Ligands: NH2
Pockets: 2 · best druggability 0.36

Structure

solid-state nmr · 1 distinct chain · 0% helix, 80% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H	MAX1 peptide	protein	20	0% helix, 80% strand	—

Ligands and binding sites

NH2 · Amino group · ion · 8 copies · chains A, B, C, D, E, F, G, H

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

Pockets

2 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	63	0.36	0.78	12	empty
2	64	0.36	0.78	18	empty

Interfaces

16 interfaces between chains.

B–F · 466 Å² buried · 0 hydrogen bonds · protein-protein
E–F · 458 Å² buried · 9 hydrogen bonds · protein-protein
A–B · 449 Å² buried · 13 hydrogen bonds · protein-protein
B–C · 446 Å² buried · 11 hydrogen bonds · protein-protein
C–D · 442 Å² buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 d-amino (D-amino acid).

Compared structures

2N1E · MAX1 peptide fibril · the same entry in another collection · chain A against A, 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
Elsewhere: RCSB PDB 2N1E · PDBe 2N1E

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