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Changing the determinants of protein stability from covalent to non- covalent interactions by in-vitro evolution: a structural and energetic analysis

Analyse Changing the determinants of protein stability from covalent to non- covalent… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3DGS
Type: protein
Length: 372 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Coat protein a
UniProt: P03661
Pockets: 1 · best druggability 0.29

Structure

x-ray diffraction · 2 distinct chains · 5% helix, 42% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Coat protein a	protein	186	6% helix, 40% strand	P03661
B	Coat protein a	protein	186	4% helix, 44% strand	P03661

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	56	0.29	0.75	18	empty

Compared structures

3DGS · Changing the determinants of protein stability from covalent to non-covalent interactions… · 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
Every structure of UniProt P03661
Elsewhere: RCSB PDB 3DGS · PDBe 3DGS · UniProt P03661

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