Research workbench

Symfoil-4V synthetic protein with T30E/T72E/T116E mutations, and delta his tag

Analyse Symfoil-4V synthetic protein with T30E/T72E/T116E mutations, and delta his tag in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4F34
Type: protein
Length: 492 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: De novo protein symfoil-4V
Pockets: 1 · best druggability 0.58

Structure

x-ray diffraction · 3 distinct chains · 7% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	De novo protein symfoil-4V	protein	123	7% helix, 48% strand	—
C	De novo protein symfoil-4V	protein	124	7% helix, 49% strand	—
D	De novo protein symfoil-4V	protein	122	7% helix, 46% strand	—

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	475	0.58	0.74	61	empty

Interfaces

4 interfaces between chains.

B–C · 302 Å² buried · 6 hydrogen bonds · protein-protein
B–D · 284 Å² buried · 4 hydrogen bonds · protein-protein
A–B · 176 Å² buried · 3 hydrogen bonds · protein-protein
A–D · 55 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

4F34 · Symfoil-4V synthetic protein with T30E/T72E/T116E mutations, and delta His tag · the same entry in another collection · chain C against C, 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
Elsewhere: RCSB PDB 4F34 · PDBe 4F34

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