Research workbench

Human kibra C2 domain mutant C771A

Analyse Human kibra C2 domain mutant C771A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6FB4
Type: protein
Length: 258 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein kibra
UniProt: Q8IX03
Ligands: PO4
Pockets: 1 · best druggability 0.60

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 53% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Protein kibra	protein	129	6% helix, 53% strand	Q8IX03

Ligands and binding sites

PO4 · Phosphate ion · ion · chains A, B
GOL · Glycerol · additive · 4 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	123	0.60	0.85	32	empty

Interfaces

1 interface between chains.

A–B · 959 Å² buried · 22 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

6FB4 · human KIBRA C2 domain mutant C771A · the same entry in another collection · chain A against A, TM-score 1.00
Q8IX03 · AlphaFold monomer V2.0 prediction for protein kibra (Q8IX03) · a predicted model of the same protein · chain A against A, TM-score 0.94

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 Q8IX03
Elsewhere: RCSB PDB 6FB4 · PDBe 6FB4 · UniProt Q8IX03

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