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Crystal structure of an atypical poplar thioredoxin-LIKE2.1 variant in dimeric form

Analyse Crystal structure of an atypical poplar thioredoxin-LIKE2.1 variant in dimeric… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5NYO
Type: protein
Length: 237 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thioredoxin-like protein 2.1
UniProt: I0BZV0
Ligands: SO4
Pockets: 1 · best druggability 0.28

Structure

x-ray diffraction · 2 distinct chains · 42% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thioredoxin-like protein 2.1	protein	118	41% helix, 23% strand	I0BZV0
B	Thioredoxin-like protein 2.1	protein	119	43% helix, 23% strand	I0BZV0

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · chains A, B

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	51	0.28	0.75	16	empty

Interfaces

1 interface between chains.

A–B · 583 Å² buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

5NYO · Crystal structure of an atypical poplar thioredoxin-like2.1 variant in dimeric form · the same entry in another collection · 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 I0BZV0
Elsewhere: RCSB PDB 5NYO · PDBe 5NYO · UniProt I0BZV0

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