Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2I2R

Crystal structure of the KChIP1/Kv4.3 T1 complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005249	molecular_function	voltage-gated potassium channel activity
A	0006813	biological_process	potassium ion transport
A	0008076	cellular_component	voltage-gated potassium channel complex
A	0051260	biological_process	protein homooligomerization
B	0005249	molecular_function	voltage-gated potassium channel activity
B	0006813	biological_process	potassium ion transport
B	0008076	cellular_component	voltage-gated potassium channel complex
B	0051260	biological_process	protein homooligomerization
C	0005249	molecular_function	voltage-gated potassium channel activity
C	0006813	biological_process	potassium ion transport
C	0008076	cellular_component	voltage-gated potassium channel complex
C	0051260	biological_process	protein homooligomerization
D	0005249	molecular_function	voltage-gated potassium channel activity
D	0006813	biological_process	potassium ion transport
D	0008076	cellular_component	voltage-gated potassium channel complex
D	0051260	biological_process	protein homooligomerization
E	0005509	molecular_function	calcium ion binding
F	0005509	molecular_function	calcium ion binding
G	0005509	molecular_function	calcium ion binding
H	0005509	molecular_function	calcium ion binding
I	0005249	molecular_function	voltage-gated potassium channel activity
I	0006813	biological_process	potassium ion transport
I	0008076	cellular_component	voltage-gated potassium channel complex
I	0051260	biological_process	protein homooligomerization
J	0005249	molecular_function	voltage-gated potassium channel activity
J	0006813	biological_process	potassium ion transport
J	0008076	cellular_component	voltage-gated potassium channel complex
J	0051260	biological_process	protein homooligomerization
K	0005249	molecular_function	voltage-gated potassium channel activity
K	0006813	biological_process	potassium ion transport
K	0008076	cellular_component	voltage-gated potassium channel complex
K	0051260	biological_process	protein homooligomerization
L	0005249	molecular_function	voltage-gated potassium channel activity
L	0006813	biological_process	potassium ion transport
L	0008076	cellular_component	voltage-gated potassium channel complex
L	0051260	biological_process	protein homooligomerization
M	0005509	molecular_function	calcium ion binding
N	0005509	molecular_function	calcium ion binding
O	0005509	molecular_function	calcium ion binding
P	0005509	molecular_function	calcium ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA F 501

Chain	Residue
F	ASP135
F	ASN137
F	ASP139
F	TYR141
F	GLU146

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA H 502

Chain	Residue
H	GLU146
H	ASP135
H	ASN137
H	ASP139
H	TYR141

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA E 503

Chain	Residue
E	ASP135
E	ASN137
E	ASP139
E	TYR141
E	GLU146

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA G 504

Chain	Residue
G	ASP135
G	ASN137
G	ASP139
G	TYR141
G	GLU146

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA P 505

Chain	Residue
P	ASP135
P	ASN137
P	ASP139
P	TYR141
P	GLU146

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA M 506

Chain	Residue
M	ASP135
M	ASN137
M	ASP139
M	TYR141
M	GLU146

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA N 507

Chain	Residue
N	ASP135
N	ASN137
N	ASP139
N	TYR141
N	GLU146

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA O 508

Chain	Residue
O	ASP135
O	ASN137
O	ASP139
O	TYR141
O	GLU146

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA F 509

Chain	Residue
F	ASP183
F	ASN185
F	ASP187
F	ILE189
F	GLU194

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA H 510

Chain	Residue
H	ASP183
H	ASN185
H	ASP187
H	ILE189
H	GLU194

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA E 511

Chain	Residue
E	ASP183
E	ASN185
E	ASP187
E	ILE189
E	GLU194

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA G 512

Chain	Residue
G	ASP183
G	ASN185
G	ASP187
G	ILE189
G	GLU194

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA P 513

Chain	Residue
P	ASP183
P	ASN185
P	ASP187
P	ILE189
P	GLU194

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA M 514

Chain	Residue
M	ASP183
M	ASN185
M	ASP187
M	ILE189
M	GLU194

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA N 515

Chain	Residue
N	ASP183
N	ASN185
N	ASP187
N	ILE189
N	GLU194

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA O 516

Chain	Residue
O	ASP183
O	ASN185
O	ASP187
O	ILE189
O	GLU194

site_id	BC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 601

Chain	Residue
A	HIS104
A	CYS131
A	CYS132
B	CYS110

site_id	BC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 602

Chain	Residue
B	HIS104
B	CYS131
B	CYS132
C	CYS110

site_id	CC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 603

Chain	Residue
C	HIS104
C	CYS131
C	CYS132
D	CYS110

site_id	CC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 604

Chain	Residue
A	CYS110
D	HIS104
D	CYS131
D	CYS132

site_id	CC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN I 605

Chain	Residue
J	CYS110
I	HIS104
I	CYS131
I	CYS132

site_id	CC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN J 606

Chain	Residue
J	HIS104
J	CYS131
J	CYS132
K	CYS110

site_id	CC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN K 607

Chain	Residue
K	HIS104
K	CYS131
K	CYS132
L	CYS110

site_id	CC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN L 608

Chain	Residue
I	CYS110
L	HIS104
L	CYS131
L	CYS132

site_id	CC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE NA H 701

Chain	Residue
H	GLU43
H	THR46
H	PHE48

site_id	CC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE NA F 702

Chain	Residue
F	GLU43
F	THR46
F	PHE48

site_id	CC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE NA E 703

Chain	Residue
E	GLU43
E	THR46
E	PHE48

site_id	DC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE NA G 704

Chain	Residue
G	GLU43
G	THR46
G	PHE48

Functional Information from PROSITE/UniProt

site_id	PS00018
Number of Residues	13
Details	EF_HAND_1 EF-hand calcium-binding domain. DINKDGYINkeEM

Chain	Residue	Details
E	ASP135-MET147
E	ASP183-PHE195

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	72
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU00448, ECO:0000269\|PubMed:17057713, ECO:0000269\|PubMed:17187064

Chain	Residue	Details
E	ASP135
F	ASP135
F	ASN137
F	ASP139
F	TYR141
F	GLU146
F	ASP183
F	ASN185
F	ASP187
F	GLU194
G	ASP135
E	ASN137
G	ASN137
G	ASP139
G	TYR141
G	GLU146
G	ASP183
G	ASN185
G	ASP187
G	GLU194
H	ASP135
H	ASN137
E	ASP139
H	ASP139
H	TYR141
H	GLU146
H	ASP183
H	ASN185
H	ASP187
H	GLU194
M	ASP135
M	ASN137
M	ASP139
E	TYR141
M	TYR141
M	GLU146
M	ASP183
M	ASN185
M	ASP187
M	GLU194
N	ASP135
N	ASN137
N	ASP139
N	TYR141
E	GLU146
N	GLU146
N	ASP183
N	ASN185
N	ASP187
N	GLU194
O	ASP135
O	ASN137
O	ASP139
O	TYR141
O	GLU146
E	ASP183
O	ASP183
O	ASN185
O	ASP187
O	GLU194
P	ASP135
P	ASN137
P	ASP139
P	TYR141
P	GLU146
P	ASP183
E	ASN185
P	ASN185
P	ASP187
P	GLU194
E	ASP187
E	GLU194

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)