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Crystal structure of bchu complexed with S-adenosyl-L-methionine

Analyse Crystal structure of bchu complexed with S-adenosyl-L-methionine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1X1A
Type: protein
Length: 337 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Crtf-related protein
UniProt: Q8KGE0
Ligands: SAM, SO4
Pockets: 1 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Crtf-related protein	protein	337	48% helix, 15% strand	Q8KGE0

Ligands and binding sites

SAM · S-adenosylmethionine · ligand · chains A
SO4 · Sulfate ion · ion · chains A
GOL · Glycerol · additive · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1070	0.80	0.81	92	SAM

Compared structures

1X1A · Crystal structure of BchU complexed with S-adenosyl-L-methionine · the same entry in another collection · chain A against A, TM-score 1.00
Q8KGE0 · AlphaFold monomer V2.0 prediction for bacteriochlorophyllide D C-20 methyltransferase… · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q8KGE0
Elsewhere: RCSB PDB 1X1A · PDBe 1X1A · UniProt Q8KGE0

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