MolNFT v1 · #140240 · protein

Crystal structure of ankb ankyrin repeats R8-14 in complex with autoinhibition segment ai-B

5Y4E · Ankyrin-2,ANKYRIN-2: “Crystal structure of ankb ankyrin repeats R8-14 in complex with autoinhibition segment ai-B”. X-ray diffraction, 1 ligand (SO4), 2 pockets (best druggability 0.52). MolNFT v1 #140240 on GenesisL1: 3D structure…

PDB: 5Y4E
Type: protein
Length: 464 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ankyrin-2,ANKYRIN-2
UniProt: Q01484
Ligands: SO4
Pockets: 2 · best druggability 0.52

Structure

x-ray diffraction · 2 distinct chains · 51% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ankyrin-2,ANKYRIN-2	protein	234	51% helix, 0% strand	Q01484
B	Ankyrin-2,ANKYRIN-2	protein	230	50% helix, 0% strand	Q01484

Ligands and binding sites

SO4 · Sulfate ion · ion · 18 copies · chains A, B
GOL · Glycerol · additive · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	320	0.52	0.73	41	GOL, SO4
2	105	0.46	0.79	20	empty

Interfaces

1 interface between chains.

A–B · 246 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

5Y4E · Crystal Structure of AnkB Ankyrin Repeats R8-14 in complex with autoinhibition segment… · the same entry in another collection · chain B against B, 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 Q01484
Elsewhere: RCSB PDB 5Y4E · PDBe 5Y4E · UniProt Q01484

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