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Annexin V under 2.0 mpa pressure of xenon

Analyse Annexin V under 2.0 mpa pressure of xenon in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2IE6
Type: protein
Length: 318 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Annexin A5
UniProt: P14668
Ligands: CA, SO4, XE
Pockets: 4 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 72% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Annexin A5	protein	318	72% helix, 0% strand	P14668

Ligands and binding sites

CA · Calcium ion · metal · 6 copies · chains A
SO4 · Sulfate ion · ion · 4 copies · chains A
XE · Xenon · ion · chains A

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

Pockets

4 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	94	0.51	0.83	26	SO4
2	96	0.49	0.82	20	empty
3	165	0.46	0.76	20	empty
4	58	0.35	0.78	14	empty

Compared structures

2IE6 · Annexin V under 2.0 MPa pressure of xenon · the same entry in another collection · chain A against A, TM-score 1.00
P14668 · AlphaFold monomer V2.0 prediction for annexin A5 (P14668) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P14668
Elsewhere: RCSB PDB 2IE6 · PDBe 2IE6 · UniProt P14668

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