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Crystal structure of a putative methyltransferase (BCE_1332) from bacillus cereus atcc 10987 at 1.64 a resolution

Analyse Crystal structure of a putative methyltransferase (BCE_1332) from bacillus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3CC8
Type
protein
Length
211 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Putative methyltransferase
UniProt
Q73BT6
Ligands
NI
Pockets
2 · best druggability 0.52

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APutative methyltransferaseprotein21134% helix, 27% strandQ73BT6

Ligands and binding sites

  • NI · Nickel (II) ion · metal · 2 copies · 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, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12260.520.7635NI
2730.310.7318empty

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

  • 3CC8 · Crystal structure of a putative methyltransferase (bce_1332) from bacillus cereus atcc… · the same entry in another collection · chain A against A, TM-score 1.00

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