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Crystal structure of an integrin BETA3-talin chimera

Analyse Crystal structure of an integrin BETA3-talin chimera in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1MK9
Type: protein
Length: 813 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Integrin BETA3; Talin
UniProt: P05106, P54939
Pockets: 12 · best druggability 0.81

Structure

x-ray diffraction · 7 distinct chains · 37% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Integrin BETA3	protein	13	0% helix, 15% strand	P05106
B	Talin	protein	187	40% helix, 21% strand	P54939
C	Integrin BETA3	protein	15	0% helix, 13% strand	P05106
D	Talin	protein	192	39% helix, 22% strand	P54939
E, G	Integrin BETA3	protein	14	0% helix, 21% strand	P05106
F	Talin	protein	190	38% helix, 20% strand	P54939
H	Talin	protein	188	38% helix, 21% strand	P54939

Pockets

12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	801	0.81	0.84	70	empty
2	538	0.66	0.77	52	empty
3	316	0.63	0.79	33	empty
4	315	0.63	0.79	37	empty
5	87	0.47	0.82	17	empty

Interfaces

13 interfaces between chains.

F–G · 531 Å² buried · 12 hydrogen bonds · protein-protein
E–H · 524 Å² buried · 8 hydrogen bonds · protein-protein
B–C · 517 Å² buried · 8 hydrogen bonds · protein-protein
A–D · 503 Å² buried · 10 hydrogen bonds · protein-protein
D–F · 453 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

1MK9 · Crystal structure of an integrin BETA3-talin chimera · the same entry in another collection · chain H against H, TM-score 1.00
P54939 · AlphaFold monomer V2.0 prediction for talin-1 (P54939) · a predicted model of the same protein · chain H against A, TM-score 0.97

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 P05106
Every structure of UniProt P54939
Elsewhere: RCSB PDB 1MK9 · PDBe 1MK9 · UniProt P05106 · UniProt P54939

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