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Crystal structure of striga hermonthica DWARF14 (SHD14)

Analyse Crystal structure of striga hermonthica DWARF14 (SHD14) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5Z7Z
Type: protein
Length: 529 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dwarf 14
UniProt: A0A0M5I7R9
Pockets: 2 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 46% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dwarf 14	protein	263	45% helix, 15% strand	A0A0M5I7R9
B	Dwarf 14	protein	266	48% helix, 15% strand	A0A0M5I7R9

Ligands and binding sites

PEG · Di(hydroxyethyl)ether · additive · 4 copies · chains A, B
EDO · 1,2-ethanediol · additive · 4 copies · chains A, B
GOL · Glycerol · additive · 2 copies · chains A, B

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

Pockets

2 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	182	0.78	0.92	27	empty
2	178	0.75	0.91	29	PEG

Interfaces

1 interface between chains.

A–B · 578 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

5Z7Z · Crystal structure of Striga hermonthica Dwarf14 (ShD14) · 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 A0A0M5I7R9
Elsewhere: RCSB PDB 5Z7Z · PDBe 5Z7Z · UniProt A0A0M5I7R9

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