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Human annexin V with proline substitution by thioproline

Analyse Human annexin V with proline substitution by thioproline in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1SAV
Type: protein
Length: 316 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Annexin V
UniProt: P08758
Ligands: CA
Pockets: 4 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 71% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Annexin V	protein	316	71% helix, 0% strand	P08758

Ligands and binding sites

CA · Calcium ion · metal · 5 copies · 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	184	0.56	0.80	19	empty
2	125	0.48	0.79	31	empty
3	105	0.48	0.81	22	empty
4	54	0.31	0.76	13	empty

Modifications

Observed in the structure: 5 modified (nonstandard).

Compared structures

1SAV · Human annexin V with proline substitution by thioproline · the same entry in another collection · chain A against A, TM-score 1.00
P08758 · AlphaFold monomer V2.0 prediction for annexin A5 (P08758) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 P08758
Elsewhere: RCSB PDB 1SAV · PDBe 1SAV · UniProt P08758

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