Research workbench

Katanin hexamer in the ring conformation

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

PDB: 5WCB
Type: protein
Length: 1,662 residues
Chains: 6
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Meiotic spindle formation protein mei-1
EC: 3.6.4.3
UniProt: P34808
Ligands: ATP
Pockets: 20 · best druggability 0.86

Structure

electron microscopy · 1 distinct chain · 44% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F	Meiotic spindle formation protein mei-1 (EC 3.6.4.3)	protein	277	44% helix, 5% strand	P34808

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · 5 copies · chains B, C, D, E, F

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

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1054	0.86	0.87	141	empty
2	505	0.84	0.89	85	empty
3	802	0.82	0.85	96	empty
4	597	0.82	0.87	97	empty
5	462	0.79	0.87	74	empty

Interfaces

6 interfaces between chains.

B–C · 1442 Å² buried · 17 hydrogen bonds · protein-protein
C–D · 1386 Å² buried · 26 hydrogen bonds · protein-protein
D–E · 1281 Å² buried · 19 hydrogen bonds · protein-protein
E–F · 1269 Å² buried · 17 hydrogen bonds · protein-protein
A–B · 790 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

5WCB · Katanin hexamer in the ring conformation · the same entry in another collection · chain C against C, TM-score 1.00
P34808 · AlphaFold monomer V2.0 prediction for meiotic spindle formation protein mei-1 (P34808) · a predicted model of the same protein · chain A against A, TM-score 0.76

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 P34808
Elsewhere: RCSB PDB 5WCB · PDBe 5WCB · UniProt P34808

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