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Crystal structure of the third tudor domain of qin

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

PDB: 7OC3
Type: protein
Length: 421 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Qin
UniProt: Q9VE55
Ligands: PO4
Pockets: 5 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 24% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Qin	protein	212	23% helix, 38% strand	Q9VE55
B	Qin	protein	209	24% helix, 38% strand	Q9VE55

Ligands and binding sites

PO4 · Phosphate ion · ion · chains A

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

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	825	0.71	0.77	63	empty
2	157	0.47	0.77	21	empty
3	150	0.45	0.76	21	empty
4	58	0.27	0.73	12	empty
5	55	0.27	0.74	22	empty

Interfaces

1 interface between chains.

A–B · 1024 Å² buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 14 modified, 2 disulfide (engineered, disulfide).

Compared structures

7OC3 · Crystal structure of the third tudor domain of Qin · 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 Q9VE55
Elsewhere: RCSB PDB 7OC3 · PDBe 7OC3 · UniProt Q9VE55

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