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Functional and structural aspects of poplar cytosolic and plastidial type a methionine sulfoxide reductases

Analyse Functional and structural aspects of poplar cytosolic and plastidial type a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2J89
Type: protein
Length: 183 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Methionine sulfoxide reductase a
UniProt: Q6QPJ4
Pockets: 1 · best druggability 0.26

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Methionine sulfoxide reductase a	protein	183	25% helix, 22% strand	Q6QPJ4

Ligands and binding sites

BME · Beta-mercaptoethanol · additive · 3 copies · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	58	0.26	0.73	13	empty

Modifications

Observed in the structure: 3 covalent, 1 modified (additive adduct, oxidation).

Compared structures

2J89 · Functional and structural aspects of poplar cytosolic and plastidial type A methionine… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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Every structure of UniProt Q6QPJ4
Elsewhere: RCSB PDB 2J89 · PDBe 2J89 · UniProt Q6QPJ4

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