Potassium in PDB 9j0z: Cryo-Em Structure of the Guard Cell Potassium Channel Gork N50 Deletion

Potassium Binding Sites:

The binding sites of Potassium atom in the Cryo-Em Structure of the Guard Cell Potassium Channel Gork N50 Deletion (pdb code 9j0z). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 4 binding sites of Potassium where determined in the Cryo-Em Structure of the Guard Cell Potassium Channel Gork N50 Deletion, PDB code: 9j0z:
Jump to Potassium binding site number: 1; 2; 3; 4;

Potassium binding site 1 out of 4 in 9j0z

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Potassium Binding Sites List in 9j0z

Potassium binding site 1 out of 4 in the Cryo-Em Structure of the Guard Cell Potassium Channel Gork N50 Deletion

Mono view

Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Cryo-Em Structure of the Guard Cell Potassium Channel Gork N50 Deletion within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:K901 b:30.0 occ:1.00	K	A:K902	2.3	30.0	1.0
	O	D:THR271	2.5	65.1	1.0
	O	C:THR271	2.6	65.6	1.0
	O	B:THR271	2.6	63.9	1.0
	O	A:THR271	2.6	65.4	1.0
	OG1	C:THR271	3.5	65.6	1.0
	OG1	D:THR271	3.5	65.1	1.0
	OG1	A:THR271	3.6	65.4	1.0
	OG1	B:THR271	3.7	63.9	1.0
	C	D:THR271	3.7	65.1	1.0
	C	C:THR271	3.7	65.6	1.0
	C	B:THR271	3.8	63.9	1.0
	C	A:THR271	3.8	65.4	1.0
	CB	C:THR271	3.8	65.6	1.0
	CB	B:THR271	3.8	63.9	1.0
	CB	D:THR271	3.9	65.1	1.0
	CB	A:THR271	3.9	65.4	1.0
	CA	C:THR271	4.4	65.6	1.0
	CA	D:THR271	4.4	65.1	1.0
	CA	B:THR271	4.5	63.9	1.0
	CA	A:THR271	4.5	65.4	1.0
	N	D:VAL272	4.7	62.6	1.0
	O	C:VAL272	4.7	62.1	1.0
	N	C:VAL272	4.7	62.1	1.0
	N	B:VAL272	4.7	62.1	1.0
	O	A:VAL272	4.7	62.7	1.0
	O	D:VAL272	4.8	62.6	1.0
	CA	D:VAL272	4.8	62.6	1.0
	O	B:VAL272	4.8	62.1	1.0
	N	A:VAL272	4.8	62.7	1.0
	CA	C:VAL272	4.8	62.1	1.0
	CA	B:VAL272	4.9	62.1	1.0
	CA	A:VAL272	4.9	62.7	1.0

Potassium binding site 2 out of 4 in 9j0z

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Potassium Binding Sites List in 9j0z

Potassium binding site 2 out of 4 in the Cryo-Em Structure of the Guard Cell Potassium Channel Gork N50 Deletion

Mono view

Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Cryo-Em Structure of the Guard Cell Potassium Channel Gork N50 Deletion within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:K902 b:30.0 occ:1.00	K	A:K901	2.3	30.0	1.0
	O	D:THR271	2.7	65.1	1.0
	O	B:THR271	2.7	63.9	1.0
	O	C:THR271	2.7	65.6	1.0
	K	A:K903	2.8	30.0	1.0
	O	A:THR271	2.8	65.4	1.0
	O	A:VAL272	2.9	62.7	1.0
	O	C:VAL272	2.9	62.1	1.0
	O	D:VAL272	2.9	62.6	1.0
	O	B:VAL272	3.0	62.1	1.0
	C	D:VAL272	3.8	62.6	1.0
	C	D:THR271	3.8	65.1	1.0
	C	A:VAL272	3.8	62.7	1.0
	C	C:VAL272	3.8	62.1	1.0
	C	B:VAL272	3.8	62.1	1.0
	C	A:THR271	3.8	65.4	1.0
	C	C:THR271	3.9	65.6	1.0
	C	B:THR271	3.9	63.9	1.0
	CA	D:VAL272	4.0	62.6	1.0
	CA	B:VAL272	4.1	62.1	1.0
	CA	A:VAL272	4.1	62.7	1.0
	CA	C:VAL272	4.1	62.1	1.0
	N	D:VAL272	4.4	62.6	1.0
	N	A:VAL272	4.5	62.7	1.0
	N	B:VAL272	4.5	62.1	1.0
	N	C:VAL272	4.5	62.1	1.0
	N	D:GLY273	4.9	62.9	1.0
	N	A:GLY273	4.9	63.0	1.0
	CA	A:THR271	4.9	65.4	1.0
	CA	D:THR271	4.9	65.1	1.0
	CB	A:THR271	4.9	65.4	1.0
	N	C:GLY273	4.9	63.1	1.0
	CB	B:THR271	5.0	63.9	1.0
	N	B:GLY273	5.0	63.0	1.0
	CA	C:THR271	5.0	65.6	1.0
	CB	D:THR271	5.0	65.1	1.0
	CA	B:THR271	5.0	63.9	1.0
	CB	C:THR271	5.0	65.6	1.0

Potassium binding site 3 out of 4 in 9j0z

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Potassium Binding Sites List in 9j0z

Potassium binding site 3 out of 4 in the Cryo-Em Structure of the Guard Cell Potassium Channel Gork N50 Deletion

Mono view

Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Cryo-Em Structure of the Guard Cell Potassium Channel Gork N50 Deletion within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:K903 b:30.0 occ:1.00	O	A:VAL272	2.3	62.7	1.0
	O	D:VAL272	2.3	62.6	1.0
	O	B:VAL272	2.5	62.1	1.0
	O	C:VAL272	2.6	62.1	1.0
	K	A:K902	2.8	30.0	1.0
	O	A:GLY273	3.0	63.0	1.0
	O	C:GLY273	3.0	63.1	1.0
	O	D:GLY273	3.0	62.9	1.0
	O	B:GLY273	3.1	63.0	1.0
	C	A:VAL272	3.5	62.7	1.0
	C	D:VAL272	3.6	62.6	1.0
	K	B:K901	3.6	30.0	1.0
	C	B:VAL272	3.7	62.1	1.0
	C	A:GLY273	3.8	63.0	1.0
	C	C:VAL272	3.8	62.1	1.0
	C	D:GLY273	3.9	62.9	1.0
	C	C:GLY273	4.0	63.1	1.0
	C	B:GLY273	4.0	63.0	1.0
	CA	A:GLY273	4.1	63.0	1.0
	CA	D:GLY273	4.1	62.9	1.0
	N	A:GLY273	4.3	63.0	1.0
	N	D:GLY273	4.3	62.9	1.0
	CA	C:GLY273	4.3	63.1	1.0
	CA	B:GLY273	4.4	63.0	1.0
	N	B:GLY273	4.5	63.0	1.0
	N	C:GLY273	4.5	63.1	1.0
	CA	A:VAL272	4.6	62.7	1.0
	CA	D:VAL272	4.6	62.6	1.0
	O	D:THR271	4.7	65.1	1.0
	CA	B:VAL272	4.7	62.1	1.0
	O	B:THR271	4.7	63.9	1.0
	O	A:THR271	4.7	65.4	1.0
	O	C:THR271	4.8	65.6	1.0
	CA	C:VAL272	4.9	62.1	1.0
	N	A:TYR274	4.9	62.4	1.0
	N	D:TYR274	5.0	60.5	1.0

Potassium binding site 4 out of 4 in 9j0z

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Potassium Binding Sites List in 9j0z

Potassium binding site 4 out of 4 in the Cryo-Em Structure of the Guard Cell Potassium Channel Gork N50 Deletion

Mono view

Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 4 of Cryo-Em Structure of the Guard Cell Potassium Channel Gork N50 Deletion within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
B:K901 b:30.0 occ:1.00	O	C:TYR274	2.5	61.7	1.0
	O	B:TYR274	2.5	62.3	1.0
	O	A:GLY273	2.7	63.0	1.0
	O	D:GLY273	2.7	62.9	1.0
	O	A:TYR274	2.9	62.4	1.0
	O	B:GLY273	2.9	63.0	1.0
	O	C:GLY273	3.0	63.1	1.0
	O	D:TYR274	3.4	60.5	1.0
	C	B:TYR274	3.4	62.3	1.0
	C	C:TYR274	3.5	61.7	1.0
	C	A:TYR274	3.5	62.4	1.0
	K	A:K903	3.6	30.0	1.0
	C	D:TYR274	3.7	60.5	1.0
	C	A:GLY273	3.8	63.0	1.0
	C	D:GLY273	3.9	62.9	1.0
	CA	B:TYR274	3.9	62.3	1.0
	CA	C:TYR274	3.9	61.7	1.0
	C	B:GLY273	4.0	63.0	1.0
	CA	A:TYR274	4.0	62.4	1.0
	CA	D:TYR274	4.0	60.5	1.0
	C	C:GLY273	4.1	63.1	1.0
	N	A:TYR274	4.4	62.4	1.0
	N	B:TYR274	4.4	62.3	1.0
	N	A:GLY275	4.4	64.4	1.0
	N	D:TYR274	4.5	60.5	1.0
	N	B:GLY275	4.5	63.9	1.0
	N	C:TYR274	4.5	61.7	1.0
	N	D:GLY275	4.5	63.7	1.0
	N	C:GLY275	4.5	63.6	1.0
	CA	A:GLY275	4.7	64.4	1.0
	CA	B:GLY275	4.8	63.9	1.0
	CA	C:GLY275	4.8	63.6	1.0
	O	D:VAL272	5.0	62.6	1.0
	CA	D:GLY275	5.0	63.7	1.0
	O	B:VAL272	5.0	62.1	1.0
	O	A:VAL272	5.0	62.7	1.0

Reference:

X.Zhang, P.Zhang. Gork K+ Channel Structure and Gating Vital For Stomatal Movements To Be Published.

Page generated: Sat Aug 9 19:15:59 2025

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