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Crystal structure of CRB2 tandem tudor domains

Analyse Crystal structure of CRB2 tandem tudor domains in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2FHD
Type: protein
Length: 432 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA repair protein RHP9/CRB2
Ligands: PO4
Pockets: 2 · best druggability 0.74

Structure

x-ray diffraction · 3 distinct chains · 10% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DNA repair protein RHP9/CRB2	protein	150	9% helix, 38% strand	—
B	DNA repair protein RHP9/CRB2	protein	140	10% helix, 36% strand	—
C	DNA repair protein RHP9/CRB2	protein	142	11% helix, 35% strand	—

Ligands and binding sites

PO4 · Phosphate ion · ion · 10 copies · chains A, B, C

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

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	72	0.74	0.97	19	empty
2	390	0.61	0.77	40	PO4

Interfaces

2 interfaces between chains.

A–C · 868 Å² buried · 5 hydrogen bonds · protein-protein
A–B · 490 Å² buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 modified (engineered).

Compared structures

2FHD · Crystal structure of Crb2 tandem tudor domains · 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
Elsewhere: RCSB PDB 2FHD · PDBe 2FHD

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