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Crystal structure of DacA from Staphylococcus aureus, N166C/T172C double mutant

Analyse Crystal structure of DacA from Staphylococcus aureus, N166C/T172C double mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6GYY
Type: protein
Length: 300 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.77
Source: Staphylococcus aureus
Molecule: Diadenylate cyclase
EC: 2.7.7.85
UniProt: A0A2P7CAT2
Pockets: 1 · best druggability 0.31

Structure

x-ray diffraction · resolution 2.77 · 2 distinct chains · 36% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Diadenylate cyclase (EC 2.7.7.85)	protein	150	36% helix, 23% strand	A0A2P7CAT2
B	Diadenylate cyclase (EC 2.7.7.85)	protein	150	36% helix, 24% strand	A0A2P7CAT2

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	58	0.31	0.76	13	empty

Interfaces

1 interface between chains.

A–B · 710 Å² buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

6GYY · Crystal structure of daca from staphylococcus aureus, N166C/T172C double mutant · 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 A0A2P7CAT2
Elsewhere: RCSB PDB 6GYY · PDBe 6GYY · UniProt A0A2P7CAT2

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