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Crystal structure of the KH1-KH2 domains from human fragile X mental retardation protein

Analyse Crystal structure of the KH1-KH2 domains from human fragile X mental… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2QND
Type: protein
Length: 284 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: FMR1 protein
UniProt: Q5PQZ6
Ligands: MG
Pockets: 3 · best druggability 0.45

Structure

x-ray diffraction · 2 distinct chains · 48% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	FMR1 protein	protein	141	48% helix, 30% strand	Q5PQZ6
B	FMR1 protein	protein	143	48% helix, 31% strand	Q5PQZ6

Ligands and binding sites

MG · Magnesium ion · metal · chains A

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

Pockets

3 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	53	0.45	0.84	23	empty
2	60	0.28	0.73	16	empty
3	68	0.28	0.72	16	empty

Interfaces

1 interface between chains.

A–B · 1105 Å² buried · 28 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

2QND · Crystal Structure of the KH1-KH2 domains from human Fragile X Mental Retardation Protein · 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 Q5PQZ6
Elsewhere: RCSB PDB 2QND · PDBe 2QND · UniProt Q5PQZ6

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