5EIK

Structure of a Trimeric Intracellular Cation channel from C. elegans in the absence of Ca2+

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005267	molecular_function	potassium channel activity
A	0016020	cellular_component	membrane
A	0042802	molecular_function	identical protein binding
A	0071805	biological_process	potassium ion transmembrane transport

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	binding site for residue PT5 A 301

Chain	Residue
A	LEU64
A	ACT304
A	DMU312
A	HOH418
A	HOH428
A	LEU68
A	ILE85
A	LYS130
A	ARG134
A	ALA165
A	SER167
A	GLY168
A	THR195

---

site_id	AC2
Number of Residues	4
Details	binding site for residue CPL A 302

Chain	Residue
A	TYR103
A	TYR107
A	ARG115
A	DMU309

---

site_id	AC3
Number of Residues	4
Details	binding site for residue MG A 303

Chain	Residue
A	HIS136
A	HOH461
A	HOH463
A	HOH480

---

site_id	AC4
Number of Residues	3
Details	binding site for residue ACT A 304

Chain	Residue
A	LYS171
A	PT5301
A	ACT305

---

site_id	AC5
Number of Residues	4
Details	binding site for residue ACT A 305

Chain	Residue
A	SER42
A	HIS45
A	ASP46
A	ACT304

---

site_id	AC6
Number of Residues	2
Details	binding site for residue ACT A 306

Chain	Residue
A	HOH426
A	HOH445

---

site_id	AC7
Number of Residues	2
Details	binding site for residue ACT A 307

Chain	Residue
A	TYR28
A	ALA93

---

site_id	AC8
Number of Residues	4
Details	binding site for residue ACT A 308

Chain	Residue
A	LEU41
A	THR118
A	HOH434
A	HOH435

---

site_id	AC9
Number of Residues	4
Details	binding site for residue DMU A 309

Chain	Residue
A	TYR28
A	LEU96
A	CPL302
A	HOH410

---

site_id	AD1
Number of Residues	6
Details	binding site for residue DMU A 311

Chain	Residue
A	TYR30
A	ARG115
A	LEU116
A	ALA117
A	TRP119
A	HOH408

---

site_id	AD2
Number of Residues	12
Details	binding site for residue DMU A 312

Chain	Residue
A	PHE54
A	HIS58
A	PHE60
A	SER61
A	TRP63
A	LEU64
A	LEU158
A	ALA177
A	THR195
A	LYS196
A	VAL199
A	PT5301

---

site_id	AD3
Number of Residues	12
Details	binding site for Poly-Saccharide residues TYR A 21 through DMU A 310

Chain	Residue
A	ASP17
A	ALA18
A	GLY19
A	GLY20
A	VAL22
A	GLN23
A	LYS24
A	LEU25
A	LYS26
A	TYR30
A	PHE31
A	GLY125

---

Functional Information from PROSITE/UniProt

site_id	PS00626
Number of Residues	11
Details	RCC1_2 Regulator of chromosome condensation (RCC1) signature 2. IAAGvKHAVRI

Chain	Residue	Details
A	ILE138-ILE148

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	40
Details	TOPO_DOM: Lumenal => ECO:0000305|PubMed:27698420

Chain	Residue	Details
A	MET1-TYR28
A	GLU83-LYS90
A	PRO150-GLU151
A	SER211-ALA216

---

site_id	SWS_FT_FI2
Number of Residues	19
Details	TRANSMEM: Helical;Name=1 => ECO:0000269|PubMed:27698420

Chain	Residue	Details
A	PRO29-GLY48

---

site_id	SWS_FT_FI3
Number of Residues	30
Details	TOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:27698420

Chain	Residue	Details
A	PRO49-LYS57
A	PRO109-THR118
A	GLY179-SER192

---

site_id	SWS_FT_FI4
Number of Residues	24
Details	TRANSMEM: Discontinuously helical;Name=2 => ECO:0000269|PubMed:27698420

Chain	Residue	Details
A	HIS58-GLY82

---

site_id	SWS_FT_FI5
Number of Residues	17
Details	TRANSMEM: Helical;Name=3 => ECO:0000269|PubMed:27698420

Chain	Residue	Details
A	GLN91-SER108

---

site_id	SWS_FT_FI6
Number of Residues	30
Details	TRANSMEM: Helical;Name=4 => ECO:0000269|PubMed:27698420

Chain	Residue	Details
A	TRP119-TYR149

---

site_id	SWS_FT_FI7
Number of Residues	26
Details	TRANSMEM: Discontinuously helical;Name=5 => ECO:0000269|PubMed:27698420

Chain	Residue	Details
A	SER152-ARG178

---

site_id	SWS_FT_FI8
Number of Residues	17
Details	TRANSMEM: Helical;Name=6 => ECO:0000269|PubMed:27698420

Chain	Residue	Details
A	PHE193-HIS210

---

site_id	SWS_FT_FI9
Number of Residues	22
Details	TRANSMEM: Helical;Name=7 => ECO:0000269|PubMed:27698420

Chain	Residue	Details
A	PRO217-LEU239

---

site_id	SWS_FT_FI10
Number of Residues	3
Details	BINDING: BINDING => ECO:0007744|PDB:5EIK

Chain	Residue	Details
A	LYS130
A	ARG134
A	GLY168

---