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1.9 ångström resolution crystal structure of the protein Q9SIY3 from arabidopsis thaliana

Analyse 1.9 ångström resolution crystal structure of the protein Q9SIY3 from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3V85
Type: protein
Length: 204 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cyth-like phosphatase
UniProt: Q9SIY3
Pockets: 1 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 45% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cyth-like phosphatase	protein	204	31% helix, 45% strand	Q9SIY3

Ligands and binding sites

CIT · Citric acid · additive · chains A

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	336	0.67	0.82	42	CIT

Compared structures

3V85 · 1.9 Angstrom resolution crystal structure of the protein Q9SIY3 from Arabidopsis thaliana · the same entry in another collection · chain A against A, TM-score 1.00
Q9SIY3 · AlphaFold monomer V2.0 prediction for triphosphate tunnel metalloenzyme 3 (Q9SIY3) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q9SIY3
Elsewhere: RCSB PDB 3V85 · PDBe 3V85 · UniProt Q9SIY3

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