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Structural and biochemical characterization of the hypothetical protein SAV2348 from staphylococcus aureus.

Analyse Structural and biochemical characterization of the hypothetical protein SAV2348… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5EO4
Type: protein
Length: 462 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thioesterase
UniProt: A0A0H3JSY9
Pockets: 5 · best druggability 0.68

Structure

x-ray diffraction · 2 distinct chains · 26% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Thioesterase	protein	155	26% helix, 39% strand	A0A0H3JSY9
C	Thioesterase	protein	152	27% helix, 37% strand	A0A0H3JSY9

Pockets

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	309	0.68	0.83	40	empty
2	211	0.66	0.85	44	empty
3	145	0.62	0.85	28	empty
4	80	0.33	0.74	18	empty
5	57	0.31	0.76	14	empty

Interfaces

2 interfaces between chains.

B–C · 1790 Å² buried · 39 hydrogen bonds · protein-protein
A–B · 833 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

5EO4 · Structural and biochemical characterization of the hypothetical protein SAV2348 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 A0A0H3JSY9
Elsewhere: RCSB PDB 5EO4 · PDBe 5EO4 · UniProt A0A0H3JSY9

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