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Structure of staphylococcus aureus peptidoglycan O-acetyltransferase a (oata) C-terminal catalytic domain

Analyse Structure of staphylococcus aureus peptidoglycan O-acetyltransferase a (oata)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6VJP
Type: protein
Length: 308 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acetyltransferase
UniProt: A0A4P7P982
Ligands: NA
Pockets: 2 · best druggability 0.45

Structure

x-ray diffraction · 2 distinct chains · 49% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acetyltransferase	protein	155	49% helix, 15% strand	A0A4P7P982
B	Acetyltransferase	protein	153	48% helix, 16% strand	A0A4P7P982

Ligands and binding sites

NA · Sodium 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	123	0.45	0.77	18	empty
2	101	0.41	0.77	24	empty

Interfaces

1 interface between chains.

A–B · 443 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

6VJP · Structure of Staphylococcus aureus peptidoglycan O-acetyltransferase A (OatA) C-terminal… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt A0A4P7P982
Elsewhere: RCSB PDB 6VJP · PDBe 6VJP · UniProt A0A4P7P982

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