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Crystal structure of the DNA binding domain of fission yeast SAP1

Analyse Crystal structure of the DNA binding domain of fission yeast SAP1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6EXU
Type: protein
Length: 104 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Switch-activating protein 1
UniProt: P40847
Pockets: 1 · best druggability 0.31

Structure

x-ray diffraction · 1 distinct chain · 76% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Switch-activating protein 1	protein	104	76% helix, 0% strand	P40847

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	68	0.31	0.74	20	empty

Modifications

Observed in the structure: 4 modified (engineered, artifact).

Compared structures

6EXU · Crystal structure of the DNA binding domain of fission yeast Sap1 · the same entry in another collection · chain A against A, TM-score 1.00
P40847 · AlphaFold monomer V2.0 prediction for switch-activating protein 1 (P40847) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P40847
Elsewhere: RCSB PDB 6EXU · PDBe 6EXU · UniProt P40847

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