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Crystal structure of cbby (AT3G48420) from arabidobsis thaliana

Analyse Crystal structure of cbby (AT3G48420) from arabidobsis thaliana in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4UAV
Type: protein
Length: 246 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Haloacid dehalogenase-like hydrolase domain-containing protein AT3G48420
EC: 3.1.3.-
UniProt: Q94K71
Ligands: MG
Pockets: 1 · best druggability 0.52

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Haloacid dehalogenase-like hydrolase domain-containing protein AT3G48420 (EC 3.1.3.-)	protein	246	48% helix, 12% strand	Q94K71

Ligands and binding sites

MG · Magnesium ion · metal · 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	259	0.52	0.75	37	MG

Compared structures

4UAV · Crystal structure of CbbY (AT3G48420) from Arabidobsis thaliana · the same entry in another collection · chain A against A, TM-score 1.00
Q94K71 · AlphaFold monomer V2.0 prediction for cbby-like protein (Q94K71) · a predicted model of the same protein · 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 Q94K71
Elsewhere: RCSB PDB 4UAV · PDBe 4UAV · UniProt Q94K71

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