3IR0

Crystal Structure of Human Insulin complexed with Cu+2 metal ion

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005179	molecular_function	hormone activity
A	0005576	cellular_component	extracellular region
B	0005179	molecular_function	hormone activity
B	0005576	cellular_component	extracellular region
C	0005179	molecular_function	hormone activity
C	0005576	cellular_component	extracellular region
D	0005179	molecular_function	hormone activity
D	0005576	cellular_component	extracellular region
E	0005179	molecular_function	hormone activity
E	0005576	cellular_component	extracellular region
F	0005179	molecular_function	hormone activity
F	0005576	cellular_component	extracellular region
G	0005179	molecular_function	hormone activity
G	0005576	cellular_component	extracellular region
H	0005179	molecular_function	hormone activity
H	0005576	cellular_component	extracellular region
I	0005179	molecular_function	hormone activity
I	0005576	cellular_component	extracellular region
J	0005179	molecular_function	hormone activity
J	0005576	cellular_component	extracellular region
K	0005179	molecular_function	hormone activity
K	0005576	cellular_component	extracellular region
L	0005179	molecular_function	hormone activity
L	0005576	cellular_component	extracellular region
M	0005179	molecular_function	hormone activity
M	0005576	cellular_component	extracellular region
N	0005179	molecular_function	hormone activity
N	0005576	cellular_component	extracellular region
O	0005179	molecular_function	hormone activity
O	0005576	cellular_component	extracellular region
P	0005179	molecular_function	hormone activity
P	0005576	cellular_component	extracellular region
R	0005179	molecular_function	hormone activity
R	0005576	cellular_component	extracellular region
S	0005179	molecular_function	hormone activity
S	0005576	cellular_component	extracellular region
T	0005179	molecular_function	hormone activity
T	0005576	cellular_component	extracellular region
U	0005179	molecular_function	hormone activity
U	0005576	cellular_component	extracellular region
V	0005179	molecular_function	hormone activity
V	0005576	cellular_component	extracellular region
W	0005179	molecular_function	hormone activity
W	0005576	cellular_component	extracellular region
X	0005179	molecular_function	hormone activity
X	0005576	cellular_component	extracellular region
Y	0005179	molecular_function	hormone activity
Y	0005576	cellular_component	extracellular region

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CU B 31

Chain	Residue
B	HIS10
B	HIS10
B	HIS10
B	HOH66
B	HOH66
B	HOH66

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CU D 31

Chain	Residue
D	HOH298
D	HOH298
D	HOH298
D	HIS10
D	HIS10
D	HIS10

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CU F 31

Chain	Residue
F	HIS10
F	HIS10
F	HIS10
F	HOH54
F	HOH54
F	HOH54

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CU H 31

Chain	Residue
H	HIS10
H	HIS10
H	HIS10
H	HOH210
H	HOH210
H	HOH210

---

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CU J 31

Chain	Residue
J	HIS10
J	HIS10
J	HIS10
J	HOH33
J	HOH33
J	HOH33

---

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CU L 31

Chain	Residue
L	HIS10
L	HIS10
L	HIS10
L	HOH236
L	HOH236
L	HOH236

---

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CU N 31

Chain	Residue
N	HIS10
N	HIS10
N	HIS10

---

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CU P 31

Chain	Residue
P	HIS10
P	HIS10
P	HIS10
P	HOH267
P	HOH267
P	HOH267

---

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CU S 31

Chain	Residue
S	HIS10
S	HIS10
S	HIS10
S	HOH140
S	HOH140
S	HOH140

---

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CU U 31

Chain	Residue
U	HIS10
U	HIS10
U	HIS10
U	HOH203
U	HOH203
U	HOH203

---

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CU W 31

Chain	Residue
W	HIS10
W	HIS10
W	HIS10
W	HOH32
W	HOH32
W	HOH32

---

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CU Y 31

Chain	Residue
Y	HIS10
Y	HIS10
Y	HIS10
Y	HOH250
Y	HOH250
Y	HOH250

---

Functional Information from PROSITE/UniProt

site_id	PS00262
Number of Residues	15
Details	INSULIN Insulin family signature. CCTSiCSlyqLenyC

Chain	Residue	Details
A	CYS6-CYS20

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	240
Details	Peptide: {"description":"Insulin A chain","featureId":"PRO_0000015821"}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	348
Details	Peptide: {"description":"Insulin B chain","featureId":"PRO_0000015819"}

Chain

Residue

Details

---