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Crystal structure of the second tudor domain of human PHF20 (homodimer form)

Analyse Crystal structure of the second tudor domain of human PHF20 (homodimer form) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3P8D
Type: protein
Length: 106 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Medulloblastoma antigen mu-mb-50.72
UniProt: Q7Z5E2
Pockets: 1 · best druggability 0.38

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 53% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Medulloblastoma antigen mu-mb-50.72	protein	53	6% helix, 53% strand	Q7Z5E2

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	97	0.38	0.76	16	empty

Interfaces

1 interface between chains.

A–B · 336 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

3P8D · Crystal structure of the second Tudor domain of human PHF20 (homodimer form) · 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 Q7Z5E2
Elsewhere: RCSB PDB 3P8D · PDBe 3P8D · UniProt Q7Z5E2

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