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Crystal structure of the fha domain of the chfr mitotic checkpoint protein complexed with tungstate

Analyse Crystal structure of the fha domain of the chfr mitotic checkpoint protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1LGP
Type: protein
Length: 113 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cell cycle checkpoint protein chfr
UniProt: Q96EP1
Ligands: WO4
Pockets: 2 · best druggability 0.38

Structure

x-ray diffraction · 1 distinct chain · 3% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cell cycle checkpoint protein chfr	protein	113	3% helix, 28% strand	Q96EP1

Ligands and binding sites

WO4 · Tungstate(vi)ion · ion · chains A

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	126	0.38	0.73	24	empty
2	119	0.37	0.73	14	empty

Compared structures

1LGP · Crystal structure of the FHA domain of the Chfr mitotic checkpoint protein complexed with… · the same entry in another collection · chain A against A, TM-score 1.00
Q96EP1 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase chfr (Q96EP1) · a predicted model of the same protein · chain A against A, TM-score 0.68

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 Q96EP1
Elsewhere: RCSB PDB 1LGP · PDBe 1LGP · UniProt Q96EP1

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