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Structure of the truncated neck and C-terminal motor homology domain of VIK1 from candida glabrata

Analyse Structure of the truncated neck and C-terminal motor homology domain of VIK1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4GKP
Type: protein
Length: 483 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Spindle pole body-associated protein VIK1
UniProt: Q6FSG8
Pockets: 3 · best druggability 0.68

Structure

x-ray diffraction · 2 distinct chains · 24% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Spindle pole body-associated protein VIK1	protein	229	27% helix, 32% strand	Q6FSG8
B	Spindle pole body-associated protein VIK1	protein	254	22% helix, 30% strand	Q6FSG8

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	679	0.68	0.76	71	empty
2	119	0.57	0.84	36	empty
3	113	0.43	0.77	24	empty

Interfaces

1 interface between chains.

A–B · 369 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

4GKP · Structure of the truncated neck and C-terminal motor homology domain of ViK1 from Candida… · 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 Q6FSG8
Elsewhere: RCSB PDB 4GKP · PDBe 4GKP · UniProt Q6FSG8

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