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Cryo-EM single particle 3D reconstruction of the native conformation of E. COLI alpha-2-macroglobulin (ecam)

Analyse Cryo-EM single particle 3D reconstruction of the native conformation of E. COLI… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5A42
Type: protein
Length: 1,597 residues
Chains: 1
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized lipoprotein yfhm
UniProt: P76578
Pockets: 19 · best druggability 0.80

Structure

electron microscopy · 1 distinct chain · 16% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uncharacterized lipoprotein yfhm	protein	1597	16% helix, 37% strand	P76578

Pockets

19 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1006	0.80	0.82	63	empty
2	686	0.78	0.83	60	empty
3	1094	0.77	0.79	106	empty
4	551	0.72	0.80	62	empty
5	485	0.68	0.79	40	empty

Compared structures

5A42 · Cryo-EM single particle 3D reconstruction of the native conformation of E. coli… · the same entry in another collection · chain A against A, TM-score 1.00
P76578 · AlphaFold monomer V2.0 prediction for alpha-2-macroglobulin (P76578) · a predicted model of the same protein · chain A against A, TM-score 0.53

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 P76578
Elsewhere: RCSB PDB 5A42 · PDBe 5A42 · UniProt P76578

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