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Crystal structure of rat annexin A11

Analyse Crystal structure of rat annexin A11 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6TU2
Type: protein
Length: 942 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Annexin
UniProt: Q5XI77
Ligands: CA
Pockets: 14 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 73% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Annexin	protein	314	73% helix, 0% strand	Q5XI77

Ligands and binding sites

CA · Calcium ion · metal · 10 copies · chains A, B, C

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

Pockets

14 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	733	0.66	0.75	69	empty
2	392	0.59	0.76	26	empty
3	250	0.59	0.80	43	empty
4	266	0.59	0.79	43	empty
5	357	0.51	0.73	33	CA

Interfaces

3 interfaces between chains.

B–C · 329 Å² buried · 2 hydrogen bonds · protein-protein
A–B · 185 Å² buried · 4 hydrogen bonds · protein-protein
A–C · 152 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

6TU2 · Crystal structure of rat annexin A11 · 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 Q5XI77
Elsewhere: RCSB PDB 6TU2 · PDBe 6TU2 · UniProt Q5XI77

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