MolNFT v1 · #115875 · protein

Crystal structure of de novo designed helical repeat protein DHR54

5CWL: “Crystal structure of de novo designed helical repeat protein DHR54”. X-ray diffraction, 1 ligand (NA), 3 pockets (best druggability 0.81). MolNFT v1 #115875 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5CWL
Type: protein
Length: 352 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Designed helical repeat protein
Ligands: NA
Pockets: 3 · best druggability 0.81

Structure

x-ray diffraction · 2 distinct chains · 90% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Designed helical repeat protein	protein	177	90% helix, 0% strand	—
B	Designed helical repeat protein	protein	175	90% helix, 0% strand	—

Ligands and binding sites

NA · Sodium ion · metal · chains A
PGE · Triethylene glycol · additive · chains A
PG4 · Tetraethylene glycol · additive · chains A

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

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	655	0.81	0.86	66	empty
2	181	0.62	0.83	32	empty
3	75	0.33	0.75	16	empty

Interfaces

1 interface between chains.

A–B · 805 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

5CWL · Crystal structure of de novo designed helical repeat protein DHR54 · 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 5CWL · PDBe 5CWL

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