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Structure of the H1 domain of human KCTD8

Analyse Structure of the H1 domain of human KCTD8 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6G57
Type: protein
Length: 360 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: BTB/POZ domain-containing protein KCTD8
UniProt: Q6ZWB6
Pockets: 2 · best druggability 0.49

Structure

x-ray diffraction · 4 distinct chains · 21% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	BTB/POZ domain-containing protein KCTD8	protein	97	22% helix, 48% strand	Q6ZWB6
B	BTB/POZ domain-containing protein KCTD8	protein	93	24% helix, 49% strand	Q6ZWB6
C	BTB/POZ domain-containing protein KCTD8	protein	88	22% helix, 51% strand	Q6ZWB6
D	BTB/POZ domain-containing protein KCTD8	protein	82	15% helix, 43% strand	Q6ZWB6

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	79	0.49	0.83	16	empty
2	62	0.38	0.79	16	empty

Interfaces

6 interfaces between chains.

B–D · 928 Å² buried · 10 hydrogen bonds · protein-protein
A–B · 478 Å² buried · 11 hydrogen bonds · protein-protein
C–D · 438 Å² buried · 13 hydrogen bonds · protein-protein
A–C · 230 Å² buried · 4 hydrogen bonds · protein-protein
B–C · 130 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

6G57 · Structure of the H1 domain of human KCTD8 · the same entry in another collection · chain D against D, TM-score 1.00
Q6ZWB6 · AlphaFold monomer V2.0 prediction for BTB/POZ domain-containing protein KCTD8 (Q6ZWB6) · a predicted model of the same protein · chain C against A, TM-score 0.87

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 Q6ZWB6
Elsewhere: RCSB PDB 6G57 · PDBe 6G57 · UniProt Q6ZWB6

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