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2.2 ångström resolution crystal structure of superantigen-like protein from staphylococcus aureus subsp. aureus nctc 8325.

Analyse 2.2 ångström resolution crystal structure of superantigen-like protein from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3R2T
Type: protein
Length: 389 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative uncharacterized protein
UniProt: Q2G2X9
Ligands: SO4
Pockets: 2 · best druggability 0.44

Structure

x-ray diffraction · 2 distinct chains · 17% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative uncharacterized protein	protein	195	17% helix, 40% strand	Q2G2X9
B	Putative uncharacterized protein	protein	194	17% helix, 40% strand	Q2G2X9

Ligands and binding sites

SO4 · Sulfate ion · ion · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	140	0.44	0.76	26	empty
2	173	0.43	0.74	29	empty

Interfaces

1 interface between chains.

A–B · 364 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

3R2T · 2.2 Angstrom Resolution Crystal Structure of Superantigen-like Protein from… · 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
Every structure of UniProt Q2G2X9
Elsewhere: RCSB PDB 3R2T · PDBe 3R2T · UniProt Q2G2X9

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