MolNFT v1 · #184613 · protein

Major seeded in vitro fibril morphology from murine SAA1.1 protein

7OVT · Serum amyloid a-2 protein: “Major seeded in vitro fibril morphology from murine SAA1.1 protein”. Electron microscopy, 1 pocket (best druggability 0.30). MolNFT v1 #184613 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7OVT
Type: protein
Length: 828 residues
Chains: 12
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Serum amyloid a-2 protein
UniProt: P05367
Pockets: 1 · best druggability 0.30

Structure

electron microscopy · 1 distinct chain · 0% helix, 70% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J, K, L	Serum amyloid a-2 protein	protein	69	0% helix, 70% strand	P05367

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	105	0.30	0.72	12	empty

Interfaces

29 interfaces between chains.

J–L · 3035 Å² buried · 101 hydrogen bonds · protein-protein
H–J · 3034 Å² buried · 101 hydrogen bonds · protein-protein
D–F · 3032 Å² buried · 101 hydrogen bonds · protein-protein
C–E · 3030 Å² buried · 101 hydrogen bonds · protein-protein
F–H · 3030 Å² buried · 101 hydrogen bonds · protein-protein

Compared structures

7OVT · major seeded in vitro fibril morphology from murine SAA1.1 protein · 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 P05367
Elsewhere: RCSB PDB 7OVT · PDBe 7OVT · UniProt P05367

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