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Crystal structure of tssk

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

PDB: 5Y0E
Type: protein
Length: 1,307 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tssk
Ligands: SO4
Pockets: 20 · best druggability 0.88

Structure

x-ray diffraction · 3 distinct chains · 32% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tssk	protein	442	33% helix, 27% strand	—
B	Tssk	protein	440	33% helix, 27% strand	—
C	Tssk	protein	425	31% helix, 27% strand	—

Ligands and binding sites

SO4 · Sulfate ion · ion · 5 copies · chains A, B, C

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

Pockets

20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1105	0.88	0.89	103	SO4
2	94	0.78	0.98	16	empty
3	61	0.74	0.99	15	empty
4	494	0.72	0.82	72	empty
5	379	0.72	0.84	53	empty

Interfaces

3 interfaces between chains.

A–B · 3553 Å² buried · 33 hydrogen bonds · protein-protein
B–C · 3004 Å² buried · 41 hydrogen bonds · protein-protein
A–C · 2981 Å² buried · 37 hydrogen bonds · protein-protein

Compared structures

5Y0E · Crystal structure of TssK · the same entry in another collection · chain C against C, 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
Elsewhere: RCSB PDB 5Y0E · PDBe 5Y0E

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