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Crystal structure of RTT109 from Candida albicans

Analyse Crystal structure of RTT109 from Candida albicans in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7BX0
Type: protein
Length: 312 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.5
Source: Candida albicans (strain SC5314 / ATCC MYA-2876)
Molecule: Histone acetyltransferase RTT109
EC: 2.3.1.48
UniProt: Q5AAJ8
Pockets: 5 · best druggability 0.73

Structure

x-ray diffraction · resolution 1.5 · 1 distinct chain · 30% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Histone acetyltransferase RTT109 (EC 2.3.1.48)	protein	312	30% helix, 28% strand	Q5AAJ8

Pockets

5 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	245	0.73	0.87	40	empty
2	89	0.36	0.75	22	empty
3	64	0.34	0.76	15	empty
4	50	0.32	0.77	12	empty
5	66	0.28	0.73	17	empty

Modifications

Observed in the structure: 6 modified (engineered, acetylation).

Compared structures

7BX0 · Crystal structure of RTT109 from candida albicans · the same entry in another collection · chain A against A, TM-score 1.00
Q5AAJ8 · AlphaFold monomer V2.0 prediction for histone acetyltransferase RTT109 (Q5AAJ8) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q5AAJ8
Elsewhere: RCSB PDB 7BX0 · PDBe 7BX0 · UniProt Q5AAJ8

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