3GKY

The Structural Basis of an ER Stress-Associated Bottleneck in a Protein Folding Landscape

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

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	HOH89
B	HOH89
B	HOH89
B	ZN31
B	ZN31
B	ZN31

---

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE IPH C 100

Chain	Residue
C	CYS6
C	SER9
C	ILE10
C	CYS11
C	HOH51
D	HIS5
D	HIS10
D	LEU11

---

site_id	AC4
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	AC5
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

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	CYS6-CYS20

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	40
Details	Peptide: {"description":"Insulin A chain","featureId":"PRO_0000015881"}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	58
Details	Peptide: {"description":"Insulin B chain","featureId":"PRO_0000015879"}

Chain

Residue

Details

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