MolNFT v1 · #144538 · protein

LARC2, the C-terminal domain of a cyclometallase involved in the synthesis of the npn cofactor of lactate racemase, apo form

6BWO · Pyridinium-3,5-bisthiocarboxylic acid mononucleotide nickel…: “LARC2, the C-terminal domain of a cyclometallase involved in the synthesis of the npn cofactor of lactate…”. X-ray diffraction, 1 pocket (best druggability 0.34). MolNFT…

PDB: 6BWO
Type: protein
Length: 288 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pyridinium-3,5-bisthiocarboxylic acid mononucleotide nickel insertion protein
UniProt: F9UST1
Pockets: 1 · best druggability 0.34

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 42% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Pyridinium-3,5-bisthiocarboxylic acid mononucleotide nickel insertion protein	protein	144	34% helix, 42% strand	F9UST1

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	61	0.34	0.77	14	empty

Interfaces

1 interface between chains.

A–B · 784 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

6BWO · LarC2, the C-terminal domain of a cyclometallase involved in the synthesis of the NPN… · the same entry in another collection · chain A against A, TM-score 1.00
F9UST1 · AlphaFold monomer V2.0 prediction for pyridinium-3,5-bisthiocarboxylic acid… · a predicted model of the same protein · chain A against A, TM-score 0.88

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 F9UST1
Elsewhere: RCSB PDB 6BWO · PDBe 6BWO · UniProt F9UST1

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