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Crystal structure of arabidopsis NRG1.1 cc-R domain K94E/K96E/R99E/K100E/R103E/K106E/K110E mutant

Analyse Crystal structure of arabidopsis NRG1.1 cc-R domain… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7L7V
Type: protein
Length: 665 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Probable disease resistance protein AT5G66900
UniProt: Q9FKZ1
Pockets: 5 · best druggability 0.67

Structure

x-ray diffraction · 6 distinct chains · 77% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Probable disease resistance protein AT5G66900	protein	121	74% helix, 2% strand	Q9FKZ1
B	Probable disease resistance protein AT5G66900	protein	109	83% helix, 0% strand	Q9FKZ1
C	Probable disease resistance protein AT5G66900	protein	109	78% helix, 0% strand	Q9FKZ1
D	Probable disease resistance protein AT5G66900	protein	102	78% helix, 0% strand	Q9FKZ1
E	Probable disease resistance protein AT5G66900	protein	108	78% helix, 0% strand	Q9FKZ1
F	Probable disease resistance protein AT5G66900	protein	116	73% helix, 2% strand	Q9FKZ1

Pockets

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	467	0.67	0.79	32	empty
2	132	0.58	0.83	20	empty
3	101	0.54	0.83	20	empty
4	205	0.50	0.76	26	empty
5	95	0.35	0.74	19	empty

Interfaces

9 interfaces between chains.

A–B · 412 Å² buried · 4 hydrogen bonds · protein-protein
A–E · 313 Å² buried · 2 hydrogen bonds · protein-protein
B–D · 312 Å² buried · 1 hydrogen bond · protein-protein
C–D · 307 Å² buried · 1 hydrogen bond · protein-protein
A–F · 300 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

7L7V · Crystal structure of Arabidopsis NRG1.1 CC-R domain… · the same entry in another collection · chain F against F, TM-score 1.00
Q9FKZ1 · AlphaFold monomer V2.0 prediction for probable disease resistance protein AT5G66900… · a predicted model of the same protein · chain B against A, TM-score 0.92

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 Q9FKZ1
Elsewhere: RCSB PDB 7L7V · PDBe 7L7V · UniProt Q9FKZ1

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