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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: 3M71
Type: protein
Length: 308 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tellurite resistance protein teha homolog
UniProt: P44741
Pockets: 8 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 81% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tellurite resistance protein teha homolog	protein	308	81% 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

8 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	231	0.64	0.83	32	empty
2	296	0.63	0.80	42	empty
3	97	0.56	0.84	14	empty
4	83	0.39	0.76	13	empty
5	98	0.36	0.74	18	empty

Compared structures

3M71 · 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 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 P44741
Elsewhere: RCSB PDB 3M71 · PDBe 3M71 · UniProt P44741

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