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Crystal structure of arabidopsis thaliana profilin 3

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

PDB
6IQK
Type
protein
Length
1,641 residues
Chains
11
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Profilin-5; ATPRF3
UniProt
Q9FE63
Pockets
20 · best druggability 0.75

Structure

x-ray diffraction · 5 distinct chains · 23% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, C, E, GProfilin-5protein13731% helix, 32% strandQ9FE63
B, DProfilin-5protein13830% helix, 32% strandQ9FE63
F, J, HProfilin-5protein13928% helix, 32% strandQ9FE63
IProfilin-5protein13628% helix, 30% strandQ9FE63
KATPRF3protein2649% helix, 2% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18980.750.7893empty
24110.640.7842empty
3660.600.9020empty
43680.600.7641empty
5710.590.9019empty

Interfaces

16 interfaces between chains.

  • E–I · 616 Ų buried · 10 hydrogen bonds · protein-protein
  • A–G · 606 Ų buried · 12 hydrogen bonds · protein-protein
  • C–D · 574 Ų buried · 2 hydrogen bonds · protein-protein
  • F–H · 560 Ų buried · 7 hydrogen bonds · protein-protein
  • D–H · 553 Ų buried · 10 hydrogen bonds · protein-protein

Compared structures

  • 6IQK · crystal structure of Arabidopsis thaliana Profilin 3 · the same entry in another collection · chain K against K, TM-score 1.00
  • Q9FE63 · AlphaFold monomer V2.0 prediction for profilin-3 (Q9FE63) · a predicted model of the same protein · chain I against A, TM-score 0.94

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