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Crystal structure of plant SLAC1 homolog teha

Analyse Crystal structure of plant SLAC1 homolog teha in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3M73
Type: protein
Length: 313 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tellurite resistance protein teha homolog
UniProt: P44741
Pockets: 7 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 80% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tellurite resistance protein teha homolog	protein	313	80% helix, 0% strand	P44741

Ligands and binding sites

BOG · octyl beta-D-glucopyranoside · additive · 4 copies · chains A

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

Pockets

7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	262	0.69	0.84	37	empty
2	325	0.65	0.80	37	empty
3	116	0.55	0.82	15	empty
4	75	0.37	0.76	11	empty
5	107	0.36	0.73	20	empty

Compared structures

3M73 · Crystal Structure of Plant SLAC1 homolog TehA · the same entry in another collection · chain A against A, TM-score 1.00
P44741 · AlphaFold monomer V2.0 prediction for tellurite resistance protein teha homolog (P44741) · 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 P44741
Elsewhere: RCSB PDB 3M73 · PDBe 3M73 · UniProt P44741

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