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Structure of pyrococcus horikoshii SAM hydroxide adenosyltransferase in complex with sah

Analyse Structure of pyrococcus horikoshii SAM hydroxide adenosyltransferase in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2WR8
Type: protein
Length: 258 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative uncharacterized protein PH0463
UniProt: O58212
Ligands: SAH
Pockets: 2 · best druggability 0.34

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative uncharacterized protein PH0463	protein	258	26% helix, 31% strand	O58212

Ligands and binding sites

SAH · S-adenosyl-L-homocysteine · ligand · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	73	0.34	0.75	14	empty
2	50	0.25	0.73	14	empty

Compared structures

2WR8 · Structure of Pyrococcus horikoshii SAM hydroxide adenosyltransferase in complex with SAH · the same entry in another collection · chain A against A, TM-score 1.00
O58212 · AlphaFold monomer V2.0 prediction for S-adenosyl-L-methionine hydrolase… · a predicted model of the same protein · chain A against A, TM-score 0.97

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 O58212
Elsewhere: RCSB PDB 2WR8 · PDBe 2WR8 · UniProt O58212

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