Research workbench

Annexin A13A

Analyse Annexin A13A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6B3I
Type: protein
Length: 911 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Annexin
UniProt: Q6FHB6
Pockets: 18 · best druggability 0.56

Structure

x-ray diffraction · 2 distinct chains · 74% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Annexin	protein	304	74% helix, 0% strand	Q6FHB6
B	Annexin	protein	303	75% helix, 0% strand	Q6FHB6

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 6 copies · chains A, B, C

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	280	0.56	0.77	30	empty
2	83	0.50	0.84	22	empty
3	63	0.47	0.84	24	empty
4	94	0.47	0.81	21	EDO
5	64	0.44	0.82	19	empty

Interfaces

2 interfaces between chains.

A–B · 1990 Å² buried · 23 hydrogen bonds · protein-protein
B–C · 735 Å² buried · 16 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

6B3I · Annexin A13a · 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 Q6FHB6
Elsewhere: RCSB PDB 6B3I · PDBe 6B3I · UniProt Q6FHB6

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.