MolNFT v1 · #42833 · protein

Insights into function, catalytic mechanism and fold evolution of mouse selenoprotein methionine sulfoxide reductase B1 through structural analysis

2KV1 · Methionine-R-sulfoxide reductase B1: “Insights into function, catalytic mechanism and fold evolution of mouse selenoprotein methionine sulfoxide…”. Solution nmr, 1 ligand (ZN), 2 pockets (best druggability 0.69). MolNFT v1 #42833 on…

PDB: 2KV1
Type: protein
Length: 124 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Methionine-R-sulfoxide reductase B1
EC: 1.8.4.-
UniProt: Q9JLC3
Ligands: ZN
Pockets: 2 · best druggability 0.69

Structure

solution nmr · 1 distinct chain · 2% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Methionine-R-sulfoxide reductase B1 (EC 1.8.4.-)	protein	124	2% helix, 20% strand	Q9JLC3

Ligands and binding sites

ZN · Zinc ion · metal · chains A

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

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	208	0.69	0.86	33	empty
2	307	0.55	0.75	37	empty

Compared structures

2KV1 · Insights into Function, Catalytic Mechanism and Fold Evolution of Mouse Selenoprotein… · 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 Q9JLC3
Elsewhere: RCSB PDB 2KV1 · PDBe 2KV1 · UniProt Q9JLC3

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