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Structure of a new family of artificial alpha helicoidal repeat proteins (alpha-rep) based on thermostable heat-like repeats

Analyse Structure of a new family of artificial alpha helicoidal repeat proteins… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3LTM
Type: protein
Length: 367 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alpha-REP4
Pockets: 1 · best druggability 0.80

Structure

x-ray diffraction · 2 distinct chains · 79% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha-REP4	protein	185	78% helix, 0% strand	—
B	Alpha-REP4	protein	182	79% helix, 0% strand	—

Ligands and binding sites

GOL · Glycerol · additive · 2 copies · chains A, B
1PE · Pentaethylene glycol · additive · chains A, B
12P · Dodecaethylene glycol · additive · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

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	1150	0.80	0.81	100	1PE, 12P, GOL

Interfaces

1 interface between chains.

A–B · 1156 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

3LTM · Structure of a new family of artificial alpha helicoidal repeat proteins (alpha-Rep)… · 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 3LTM · PDBe 3LTM

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