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Crystal structure of arabidopsis DWARF14 orthologue, ATD14

Analyse Crystal structure of arabidopsis DWARF14 orthologue, ATD14 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4IH4
Type: protein
Length: 1,044 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: AT3G03990/T11I18_10
UniProt: Q9SQR3
Pockets: 8 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	AT3G03990/T11I18_10	protein	261	42% helix, 10% strand	Q9SQR3

Pockets

8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	213	0.74	0.89	34	empty
2	208	0.74	0.89	34	empty
3	196	0.73	0.89	34	empty
4	206	0.73	0.89	34	empty
5	331	0.56	0.76	46	empty

Interfaces

3 interfaces between chains.

A–B · 571 Å² buried · 6 hydrogen bonds · protein-protein
C–D · 569 Å² buried · 5 hydrogen bonds · protein-protein
B–D · 466 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

4IH4 · Crystal structure of Arabidopsis DWARF14 orthologue, AtD14 · the same entry in another collection · chain D against D, TM-score 1.00
Q9SQR3 · AlphaFold monomer V2.0 prediction for strigolactone esterase D14 (Q9SQR3) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q9SQR3
Elsewhere: RCSB PDB 4IH4 · PDBe 4IH4 · UniProt Q9SQR3

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