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Helical assembly of a designed anbu protein

Analyse Helical assembly of a designed anbu protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5LOY
Type: protein
Length: 916 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Designed anbu protein
Pockets: 10 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Designed anbu protein	protein	229	32% helix, 30% strand	—

Pockets

10 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	99	0.78	0.98	20	empty
2	90	0.77	0.98	20	empty
3	1043	0.77	0.79	107	empty
4	331	0.65	0.80	45	empty
5	440	0.58	0.74	67	empty

Interfaces

5 interfaces between chains.

B–D · 2154 Å² buried · 19 hydrogen bonds · protein-protein
A–C · 2073 Å² buried · 19 hydrogen bonds · protein-protein
C–D · 696 Å² buried · 7 hydrogen bonds · protein-protein
A–B · 663 Å² buried · 7 hydrogen bonds · protein-protein
A–D · 284 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

5LOY · Helical Assembly of a Designed Anbu Protein · 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
Elsewhere: RCSB PDB 5LOY · PDBe 5LOY

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