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Two-protofilament amyloid structure of S20G variant of human amylin (iapp - islet amyloid polypeptide)

Analyse Two-protofilament amyloid structure of S20G variant of human amylin (iapp… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6ZRQ
Type: protein
Length: 276 residues
Chains: 12
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Islet amyloid polypeptide
UniProt: P10997
Pockets: 1 · best druggability 0.69

Structure

electron microscopy · 1 distinct chain · 0% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J, K, L	Islet amyloid polypeptide	protein	23	0% helix, 35% strand	P10997

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	281	0.69	0.84	39	empty

Interfaces

21 interfaces between chains.

I–K · 877 Å² buried · 24 hydrogen bonds · protein-protein
A–C · 875 Å² buried · 23 hydrogen bonds · protein-protein
J–L · 873 Å² buried · 24 hydrogen bonds · protein-protein
B–D · 872 Å² buried · 23 hydrogen bonds · protein-protein
G–I · 870 Å² buried · 23 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 modified (nonstandard).

Compared structures

6ZRQ · two-protofilament amyloid structure of S20G variant of human amylin (IAPP - islet amyloid… · 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 P10997
Elsewhere: RCSB PDB 6ZRQ · PDBe 6ZRQ · UniProt P10997

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