MolNFT v1 · #36021 · protein

Conserved hypothetical protein- streptococcus pyogenes

2ESR · Methyltransferase: “Conserved hypothetical protein- streptococcus pyogenes”. X-ray diffraction, 1 ligand (GLC), 5 pockets (best druggability 0.56). MolNFT v1 #36021 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2ESR
Type: protein
Length: 320 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Methyltransferase
EC: 2.1.1.-
Ligands: GLC
Pockets: 5 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Methyltransferase (EC 2.1.1.-)	protein	160	33% helix, 33% strand	—

Ligands and binding sites

GLC · alpha-D-glucopyranose · sugar · chains B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	102	0.56	0.85	32	empty
2	141	0.47	0.78	18	GLC
3	54	0.46	0.85	13	empty
4	116	0.41	0.76	19	empty
5	50	0.28	0.75	17	empty

Interfaces

1 interface between chains.

A–B · 884 Å² buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 modified (engineered).

Compared structures

2ESR · conserved hypothetical protein- streptococcus pyogenes · 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
Elsewhere: RCSB PDB 2ESR · PDBe 2ESR

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