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Tir-saved effector bound to CA3

Analyse Tir-saved effector bound to CA3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7QQK
Type: protein + RNA
Length: 1,744 residues
Chains: 8
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: TIR_SAVED fusion protein; RNA (5'-R(P*AP*AP*A)-3')
UniProt: A0A0M2HE71
Pockets: 17 · best druggability 0.65

Structure

electron microscopy · 2 distinct chains · 35% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	TIR_SAVED fusion protein	protein	433	35% helix, 21% strand	A0A0M2HE71
E, F, G, H	RNA (5'-R(PAPAP*A)-3')	rna	3	—	—

Pockets

17 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	298	0.65	0.81	39	empty
2	204	0.61	0.82	29	empty
3	222	0.60	0.81	33	empty
4	428	0.60	0.75	44	empty
5	137	0.58	0.83	25	empty

Interfaces

10 interfaces between chains.

C–D · 2074 Å² buried · 41 hydrogen bonds · protein-protein
B–C · 2053 Å² buried · 38 hydrogen bonds · protein-protein
A–B · 2000 Å² buried · 27 hydrogen bonds · protein-protein
D–H · 655 Å² buried · 17 hydrogen bonds · protein-nucleic
B–G · 653 Å² buried · 22 hydrogen bonds · protein-nucleic

Compared structures

7QQK · TIR-SAVED effector bound to cA3 · the same entry in another collection · chain D against D, 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 A0A0M2HE71
Elsewhere: RCSB PDB 7QQK · PDBe 7QQK · UniProt A0A0M2HE71

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