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The crystal structure of gene product SA0254 from staphylocococcus aureus subsp. aureus N315

Analyse The crystal structure of gene product SA0254 from staphylocococcus aureus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2OOI
Type: protein
Length: 315 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: SA0254 protein
UniProt: Q7A7U1
Ligands: ZN
Pockets: 2 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 20% helix, 46% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	SA0254 protein	protein	157	20% helix, 46% strand	Q7A7U1
B	SA0254 protein	protein	158	20% helix, 46% strand	Q7A7U1

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A, B

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

Pockets

2 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	58	0.71	0.97	22	ZN
2	83	0.43	0.79	16	empty

Interfaces

1 interface between chains.

A–B · 1347 Å² buried · 26 hydrogen bonds · protein-protein

Compared structures

2OOI · The crystal structure of gene product SA0254 from Staphylocococcus aureus subsp. aureus… · 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 Q7A7U1
Elsewhere: RCSB PDB 2OOI · PDBe 2OOI · UniProt Q7A7U1

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