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Crystal structure of ankb 24 ankyrin repeats in complex with ankr autoinhibition segment

Analyse Crystal structure of ankb 24 ankyrin repeats in complex with ankr… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4RLV
Type: protein
Length: 838 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ankyrin-1, ankyrin-2
UniProt: D3YTV8, Q01484
Ligands: SO4
Pockets: 3 · best druggability 0.35

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ankyrin-1, ankyrin-2	protein	838	48% helix, 0% strand	D3YTV8, Q01484

Ligands and binding sites

SO4 · Sulfate ion · ion · 9 copies · chains A

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

Pockets

3 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	74	0.35	0.76	17	empty
2	53	0.30	0.75	15	empty
3	61	0.30	0.74	14	empty

Modifications

Observed in the structure: 16 modified (engineered).

Compared structures

4RLV · Crystal Structure of AnkB 24 Ankyrin Repeats in Complex with AnkR Autoinhibition Segment · 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 D3YTV8
Every structure of UniProt Q01484
Elsewhere: RCSB PDB 4RLV · PDBe 4RLV · UniProt D3YTV8 · UniProt Q01484

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