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KH DOMAINS

Analyse KH DOMAINS in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3N89
Type: protein
Length: 656 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Defective in germ line development protein 3, isoform a
UniProt: Q95ZK7
Pockets: 7 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Defective in germ line development protein 3, isoform a	protein	337	34% helix, 28% strand	Q95ZK7
B	Defective in germ line development protein 3, isoform a	protein	319	34% helix, 29% strand	Q95ZK7

Pockets

7 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	860	0.76	0.80	72	empty
2	107	0.46	0.79	17	empty
3	102	0.42	0.77	17	empty
4	96	0.40	0.77	23	empty
5	57	0.33	0.77	15	empty

Interfaces

1 interface between chains.

A–B · 476 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

3N89 · KH domains · the same entry in another collection · chain A against A, TM-score 1.00
Q95ZK7 · AlphaFold monomer V2.0 prediction for defective in germ line development protein 3… · a predicted model of the same protein · chain B against A, TM-score 0.99

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 Q95ZK7
Elsewhere: RCSB PDB 3N89 · PDBe 3N89 · UniProt Q95ZK7

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