3P33

Insulin fibrillation is the Janus face of induced fit. A chiral clamp stabilizes the native state at the expense of activity

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

Functional Information from PDB Data

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

Chain	Residue
B	HIS10
B	HIS10
B	HIS10
B	CL32
B	CL32
B	CL32

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CL B 32

Chain	Residue
B	ZN31
B	ZN31
B	ZN31
B	HIS10
B	HIS10
B	HIS10

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN D 31

Chain	Residue
D	HIS10
D	HIS10
D	HIS10
D	CL32
D	CL32
D	CL32

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CL D 32

Chain	Residue
D	HIS10
D	HIS10
D	HIS10
D	ZN31
D	ZN31
D	ZN31

---

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN F 31

Chain	Residue
F	HIS10
F	HIS10
F	HIS10
F	CL32
F	CL32
F	CL32

---

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CL F 32

Chain	Residue
F	HIS10
F	HIS10
F	HIS10
F	ZN31
F	ZN31
F	ZN31

---

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN H 31

Chain	Residue
H	HIS10
H	HIS10
H	HIS10
H	CL32
H	CL32
H	CL32

---

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CL H 32

Chain	Residue
H	HIS10
H	HIS10
H	HIS10
H	ZN31
H	ZN31
H	ZN31

---

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE IPH A 100

Chain	Residue
A	CYS6
A	SER9
A	ILE10
A	CYS11
B	LEU11

---

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE IPH C 200

Chain	Residue
C	CYS6
C	SER9
C	CYS11
D	HIS10

---

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE IPH E 300

Chain	Residue
E	CYS6
E	SER9
E	ILE10
E	CYS11
F	HIS5
F	LEU11

---

site_id	BC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE IPH G 400

Chain	Residue
G	CYS6
G	SER9
G	ILE10
G	CYS11
H	HIS5
H	HIS10
H	LEU11

---

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	80
Details	Peptide: {"description":"Insulin A chain","featureId":"PRO_0000015821"}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	116
Details	Peptide: {"description":"Insulin B chain","featureId":"PRO_0000015819"}

Chain

Residue

Details

---