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Speg spermidine N-acetyltransferase from staphylococcus aureus in complex with spermine

Analyse Speg spermidine N-acetyltransferase from staphylococcus aureus in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7KY3
Type: protein
Length: 497 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Diamine N-acetyltransferase
UniProt: U5NVV0
Ligands: SPM
Pockets: 6 · best druggability 0.80

Structure

x-ray diffraction · 2 distinct chains · 36% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
C, A	Diamine N-acetyltransferase	protein	166	36% helix, 36% strand	U5NVV0
B	Diamine N-acetyltransferase	protein	165	36% helix, 36% strand	U5NVV0

Ligands and binding sites

SPM · Spermine · ligand · 3 copies · chains C, B, A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	804	0.80	0.83	86	SPM
2	207	0.66	0.84	28	SPM
3	188	0.63	0.83	25	empty
4	174	0.61	0.82	24	empty
5	170	0.58	0.81	23	empty

Interfaces

2 interfaces between chains.

C–B · 996 Å² buried · 20 hydrogen bonds · protein-protein
B–A · 729 Å² buried · 12 hydrogen bonds · protein-protein

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 U5NVV0
Elsewhere: RCSB PDB 7KY3 · PDBe 7KY3 · UniProt U5NVV0

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