Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5XWM

human ERp44 zinc-bound form

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003756	molecular_function	protein disulfide isomerase activity
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005783	cellular_component	endoplasmic reticulum
A	0005788	cellular_component	endoplasmic reticulum lumen
A	0005789	cellular_component	endoplasmic reticulum membrane
A	0005793	cellular_component	endoplasmic reticulum-Golgi intermediate compartment
A	0006457	biological_process	protein folding
A	0006986	biological_process	response to unfolded protein
A	0009100	biological_process	glycoprotein metabolic process
A	0009986	cellular_component	cell surface
A	0034976	biological_process	response to endoplasmic reticulum stress
A	0035580	cellular_component	specific granule lumen
A	0045454	biological_process	cell redox homeostasis
A	0070062	cellular_component	extracellular exosome
B	0003756	molecular_function	protein disulfide isomerase activity
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005783	cellular_component	endoplasmic reticulum
B	0005788	cellular_component	endoplasmic reticulum lumen
B	0005789	cellular_component	endoplasmic reticulum membrane
B	0005793	cellular_component	endoplasmic reticulum-Golgi intermediate compartment
B	0006457	biological_process	protein folding
B	0006986	biological_process	response to unfolded protein
B	0009100	biological_process	glycoprotein metabolic process
B	0009986	cellular_component	cell surface
B	0034976	biological_process	response to endoplasmic reticulum stress
B	0035580	cellular_component	specific granule lumen
B	0045454	biological_process	cell redox homeostasis
B	0070062	cellular_component	extracellular exosome
C	0003756	molecular_function	protein disulfide isomerase activity
C	0005515	molecular_function	protein binding
C	0005576	cellular_component	extracellular region
C	0005783	cellular_component	endoplasmic reticulum
C	0005788	cellular_component	endoplasmic reticulum lumen
C	0005789	cellular_component	endoplasmic reticulum membrane
C	0005793	cellular_component	endoplasmic reticulum-Golgi intermediate compartment
C	0006457	biological_process	protein folding
C	0006986	biological_process	response to unfolded protein
C	0009100	biological_process	glycoprotein metabolic process
C	0009986	cellular_component	cell surface
C	0034976	biological_process	response to endoplasmic reticulum stress
C	0035580	cellular_component	specific granule lumen
C	0045454	biological_process	cell redox homeostasis
C	0070062	cellular_component	extracellular exosome
D	0003756	molecular_function	protein disulfide isomerase activity
D	0005515	molecular_function	protein binding
D	0005576	cellular_component	extracellular region
D	0005783	cellular_component	endoplasmic reticulum
D	0005788	cellular_component	endoplasmic reticulum lumen
D	0005789	cellular_component	endoplasmic reticulum membrane
D	0005793	cellular_component	endoplasmic reticulum-Golgi intermediate compartment
D	0006457	biological_process	protein folding
D	0006986	biological_process	response to unfolded protein
D	0009100	biological_process	glycoprotein metabolic process
D	0009986	cellular_component	cell surface
D	0034976	biological_process	response to endoplasmic reticulum stress
D	0035580	cellular_component	specific granule lumen
D	0045454	biological_process	cell redox homeostasis
D	0070062	cellular_component	extracellular exosome

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue ZN A 401

Chain	Residue
A	CYS29
A	TYR78
A	CL404
C	HIS333
C	CL403

site_id	AC2
Number of Residues	4
Details	binding site for residue ZN A 402

Chain	Residue
A	HIS277
A	HIS281
C	HIS277
C	HIS281

site_id	AC3
Number of Residues	4
Details	binding site for residue ZN A 403

Chain	Residue
A	HIS299
A	HIS328
A	HIS332
A	HOH533

site_id	AC4
Number of Residues	3
Details	binding site for residue CL A 404

Chain	Residue
A	TYR78
A	ZN401
C	CL403

site_id	AC5
Number of Residues	4
Details	binding site for residue CL A 405

Chain	Residue
A	ARG329
C	TRP28
C	ZN402
C	CL404

site_id	AC6
Number of Residues	4
Details	binding site for residue ZN B 401

Chain	Residue
B	HIS277
B	HIS281
D	HIS277
D	HIS281

site_id	AC7
Number of Residues	5
Details	binding site for residue ZN B 402

Chain	Residue
B	HIS299
B	HIS328
B	HIS332
B	HOH618
B	HOH621

site_id	AC8
Number of Residues	5
Details	binding site for residue ZN B 403

Chain	Residue
B	CYS29
B	TYR78
B	CL405
D	HIS333
D	CL404

site_id	AC9
Number of Residues	3
Details	binding site for residue CL B 404

Chain	Residue
B	ARG329
D	ZN401
D	CL403

site_id	AD1
Number of Residues	3
Details	binding site for residue CL B 405

Chain	Residue
B	TYR78
B	ZN403
D	CL404

site_id	AD2
Number of Residues	4
Details	binding site for residue ZN C 401

Chain	Residue
C	HIS299
C	HIS328
C	HIS332
C	HOH629

site_id	AD3
Number of Residues	5
Details	binding site for residue ZN C 402

Chain	Residue
A	HIS333
A	CL405
C	CYS29
C	TYR78
C	CL404

site_id	AD4
Number of Residues	3
Details	binding site for residue CL C 403

Chain	Residue
A	ZN401
A	CL404
C	ARG329

site_id	AD5
Number of Residues	4
Details	binding site for residue CL C 404

Chain	Residue
A	CL405
C	TRP28
C	TYR78
C	ZN402

site_id	AD6
Number of Residues	5
Details	binding site for residue ZN D 401

Chain	Residue
B	HIS333
B	CL404
D	CYS29
D	TYR78
D	CL403

site_id	AD7
Number of Residues	4
Details	binding site for residue ZN D 402

Chain	Residue
D	HIS299
D	HIS328
D	HIS332
D	HOH639

site_id	AD8
Number of Residues	2
Details	binding site for residue CL D 403

Chain	Residue
B	CL404
D	ZN401

site_id	AD9
Number of Residues	4
Details	binding site for residue CL D 404

Chain	Residue
B	ZN403
B	CL405
D	ARG329
D	HIS333

Functional Information from PROSITE/UniProt

site_id	PS00014
Number of Residues	4
Details	ER_TARGET Endoplasmic reticulum targeting sequence. RDEL

Chain	Residue	Details
A	ARG374-LEU377

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