Research workbench

Escherichia COLI alpha-2-macroglobulin activated by porcine elastase

Analyse Escherichia COLI alpha-2-macroglobulin activated by porcine elastase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4RTD
Type: protein
Length: 1,122 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized lipoprotein yfhm
UniProt: P76578
Pockets: 17 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 18% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uncharacterized lipoprotein yfhm	protein	1122	18% helix, 36% strand	P76578

Pockets

17 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	504	0.82	0.88	55	empty
2	889	0.75	0.79	88	empty
3	165	0.74	0.91	27	empty
4	77	0.72	0.96	15	empty
5	220	0.55	0.78	41	empty

Modifications

Observed in the structure: 19 modified (engineered).

Compared structures

4RTD · Escherichia coli alpha-2-macroglobulin activated by porcine elastase · 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 0.66

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 4RTD · PDBe 4RTD · UniProt P76578

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