5E84

ATP-bound state of BiP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0005509	molecular_function	calcium ion binding
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
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	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0005925	cellular_component	focal adhesion
A	0006457	biological_process	protein folding
A	0008180	cellular_component	COP9 signalosome
A	0009986	cellular_component	cell surface
A	0016020	cellular_component	membrane
A	0016787	molecular_function	hydrolase activity
A	0016887	molecular_function	ATP hydrolysis activity
A	0019899	molecular_function	enzyme binding
A	0019904	molecular_function	protein domain specific binding
A	0021589	biological_process	cerebellum structural organization
A	0021680	biological_process	cerebellar Purkinje cell layer development
A	0021762	biological_process	substantia nigra development
A	0030291	molecular_function	protein serine/threonine kinase inhibitor activity
A	0030335	biological_process	positive regulation of cell migration
A	0030496	cellular_component	midbody
A	0030968	biological_process	endoplasmic reticulum unfolded protein response
A	0031072	molecular_function	heat shock protein binding
A	0031204	biological_process	post-translational protein targeting to membrane, translocation
A	0031333	biological_process	negative regulation of protein-containing complex assembly
A	0031398	biological_process	positive regulation of protein ubiquitination
A	0031625	molecular_function	ubiquitin protein ligase binding
A	0032991	cellular_component	protein-containing complex
A	0034663	cellular_component	endoplasmic reticulum chaperone complex
A	0034975	biological_process	protein folding in endoplasmic reticulum
A	0034976	biological_process	response to endoplasmic reticulum stress
A	0035437	biological_process	maintenance of protein localization in endoplasmic reticulum
A	0036498	biological_process	IRE1-mediated unfolded protein response
A	0036503	biological_process	ERAD pathway
A	0042026	biological_process	protein refolding
A	0042149	biological_process	cellular response to glucose starvation
A	0042470	cellular_component	melanosome
A	0043022	molecular_function	ribosome binding
A	0043066	biological_process	negative regulation of apoptotic process
A	0043231	cellular_component	intracellular membrane-bounded organelle
A	0044183	molecular_function	protein folding chaperone
A	0045296	molecular_function	cadherin binding
A	0045944	biological_process	positive regulation of transcription by RNA polymerase II
A	0051082	molecular_function	unfolded protein binding
A	0051087	molecular_function	protein-folding chaperone binding
A	0051603	biological_process	proteolysis involved in protein catabolic process
A	0051787	molecular_function	misfolded protein binding
A	0060904	biological_process	regulation of protein folding in endoplasmic reticulum
A	0070062	cellular_component	extracellular exosome
A	0140311	molecular_function	protein sequestering activity
A	1903891	biological_process	regulation of ATF6-mediated unfolded protein response
A	1903894	biological_process	regulation of IRE1-mediated unfolded protein response
A	1903895	biological_process	negative regulation of IRE1-mediated unfolded protein response
A	1903897	biological_process	regulation of PERK-mediated unfolded protein response
A	1903898	biological_process	negative regulation of PERK-mediated unfolded protein response
B	0000166	molecular_function	nucleotide binding
B	0005509	molecular_function	calcium ion binding
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005739	cellular_component	mitochondrion
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	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0005925	cellular_component	focal adhesion
B	0006457	biological_process	protein folding
B	0008180	cellular_component	COP9 signalosome
B	0009986	cellular_component	cell surface
B	0016020	cellular_component	membrane
B	0016787	molecular_function	hydrolase activity
B	0016887	molecular_function	ATP hydrolysis activity
B	0019899	molecular_function	enzyme binding
B	0019904	molecular_function	protein domain specific binding
B	0021589	biological_process	cerebellum structural organization
B	0021680	biological_process	cerebellar Purkinje cell layer development
B	0021762	biological_process	substantia nigra development
B	0030291	molecular_function	protein serine/threonine kinase inhibitor activity
B	0030335	biological_process	positive regulation of cell migration
B	0030496	cellular_component	midbody
B	0030968	biological_process	endoplasmic reticulum unfolded protein response
B	0031072	molecular_function	heat shock protein binding
B	0031204	biological_process	post-translational protein targeting to membrane, translocation
B	0031333	biological_process	negative regulation of protein-containing complex assembly
B	0031398	biological_process	positive regulation of protein ubiquitination
B	0031625	molecular_function	ubiquitin protein ligase binding
B	0032991	cellular_component	protein-containing complex
B	0034663	cellular_component	endoplasmic reticulum chaperone complex
B	0034975	biological_process	protein folding in endoplasmic reticulum
B	0034976	biological_process	response to endoplasmic reticulum stress
B	0035437	biological_process	maintenance of protein localization in endoplasmic reticulum
B	0036498	biological_process	IRE1-mediated unfolded protein response
B	0036503	biological_process	ERAD pathway
B	0042026	biological_process	protein refolding
B	0042149	biological_process	cellular response to glucose starvation
B	0042470	cellular_component	melanosome
B	0043022	molecular_function	ribosome binding
B	0043066	biological_process	negative regulation of apoptotic process
B	0043231	cellular_component	intracellular membrane-bounded organelle
B	0044183	molecular_function	protein folding chaperone
B	0045296	molecular_function	cadherin binding
B	0045944	biological_process	positive regulation of transcription by RNA polymerase II
B	0051082	molecular_function	unfolded protein binding
B	0051087	molecular_function	protein-folding chaperone binding
B	0051603	biological_process	proteolysis involved in protein catabolic process
B	0051787	molecular_function	misfolded protein binding
B	0060904	biological_process	regulation of protein folding in endoplasmic reticulum
B	0070062	cellular_component	extracellular exosome
B	0140311	molecular_function	protein sequestering activity
B	1903891	biological_process	regulation of ATF6-mediated unfolded protein response
B	1903894	biological_process	regulation of IRE1-mediated unfolded protein response
B	1903895	biological_process	negative regulation of IRE1-mediated unfolded protein response
B	1903897	biological_process	regulation of PERK-mediated unfolded protein response
B	1903898	biological_process	negative regulation of PERK-mediated unfolded protein response
C	0000166	molecular_function	nucleotide binding
C	0005509	molecular_function	calcium ion binding
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005634	cellular_component	nucleus
C	0005737	cellular_component	cytoplasm
C	0005739	cellular_component	mitochondrion
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	0005829	cellular_component	cytosol
C	0005886	cellular_component	plasma membrane
C	0005925	cellular_component	focal adhesion
C	0006457	biological_process	protein folding
C	0008180	cellular_component	COP9 signalosome
C	0009986	cellular_component	cell surface
C	0016020	cellular_component	membrane
C	0016787	molecular_function	hydrolase activity
C	0016887	molecular_function	ATP hydrolysis activity
C	0019899	molecular_function	enzyme binding
C	0019904	molecular_function	protein domain specific binding
C	0021589	biological_process	cerebellum structural organization
C	0021680	biological_process	cerebellar Purkinje cell layer development
C	0021762	biological_process	substantia nigra development
C	0030291	molecular_function	protein serine/threonine kinase inhibitor activity
C	0030335	biological_process	positive regulation of cell migration
C	0030496	cellular_component	midbody
C	0030968	biological_process	endoplasmic reticulum unfolded protein response
C	0031072	molecular_function	heat shock protein binding
C	0031204	biological_process	post-translational protein targeting to membrane, translocation
C	0031333	biological_process	negative regulation of protein-containing complex assembly
C	0031398	biological_process	positive regulation of protein ubiquitination
C	0031625	molecular_function	ubiquitin protein ligase binding
C	0032991	cellular_component	protein-containing complex
C	0034663	cellular_component	endoplasmic reticulum chaperone complex
C	0034975	biological_process	protein folding in endoplasmic reticulum
C	0034976	biological_process	response to endoplasmic reticulum stress
C	0035437	biological_process	maintenance of protein localization in endoplasmic reticulum
C	0036498	biological_process	IRE1-mediated unfolded protein response
C	0036503	biological_process	ERAD pathway
C	0042026	biological_process	protein refolding
C	0042149	biological_process	cellular response to glucose starvation
C	0042470	cellular_component	melanosome
C	0043022	molecular_function	ribosome binding
C	0043066	biological_process	negative regulation of apoptotic process
C	0043231	cellular_component	intracellular membrane-bounded organelle
C	0044183	molecular_function	protein folding chaperone
C	0045296	molecular_function	cadherin binding
C	0045944	biological_process	positive regulation of transcription by RNA polymerase II
C	0051082	molecular_function	unfolded protein binding
C	0051087	molecular_function	protein-folding chaperone binding
C	0051603	biological_process	proteolysis involved in protein catabolic process
C	0051787	molecular_function	misfolded protein binding
C	0060904	biological_process	regulation of protein folding in endoplasmic reticulum
C	0070062	cellular_component	extracellular exosome
C	0140311	molecular_function	protein sequestering activity
C	1903891	biological_process	regulation of ATF6-mediated unfolded protein response
C	1903894	biological_process	regulation of IRE1-mediated unfolded protein response
C	1903895	biological_process	negative regulation of IRE1-mediated unfolded protein response
C	1903897	biological_process	regulation of PERK-mediated unfolded protein response
C	1903898	biological_process	negative regulation of PERK-mediated unfolded protein response
D	0000166	molecular_function	nucleotide binding
D	0005509	molecular_function	calcium ion binding
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005634	cellular_component	nucleus
D	0005737	cellular_component	cytoplasm
D	0005739	cellular_component	mitochondrion
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	0005829	cellular_component	cytosol
D	0005886	cellular_component	plasma membrane
D	0005925	cellular_component	focal adhesion
D	0006457	biological_process	protein folding
D	0008180	cellular_component	COP9 signalosome
D	0009986	cellular_component	cell surface
D	0016020	cellular_component	membrane
D	0016787	molecular_function	hydrolase activity
D	0016887	molecular_function	ATP hydrolysis activity
D	0019899	molecular_function	enzyme binding
D	0019904	molecular_function	protein domain specific binding
D	0021589	biological_process	cerebellum structural organization
D	0021680	biological_process	cerebellar Purkinje cell layer development
D	0021762	biological_process	substantia nigra development
D	0030291	molecular_function	protein serine/threonine kinase inhibitor activity
D	0030335	biological_process	positive regulation of cell migration
D	0030496	cellular_component	midbody
D	0030968	biological_process	endoplasmic reticulum unfolded protein response
D	0031072	molecular_function	heat shock protein binding
D	0031204	biological_process	post-translational protein targeting to membrane, translocation
D	0031333	biological_process	negative regulation of protein-containing complex assembly
D	0031398	biological_process	positive regulation of protein ubiquitination
D	0031625	molecular_function	ubiquitin protein ligase binding
D	0032991	cellular_component	protein-containing complex
D	0034663	cellular_component	endoplasmic reticulum chaperone complex
D	0034975	biological_process	protein folding in endoplasmic reticulum
D	0034976	biological_process	response to endoplasmic reticulum stress
D	0035437	biological_process	maintenance of protein localization in endoplasmic reticulum
D	0036498	biological_process	IRE1-mediated unfolded protein response
D	0036503	biological_process	ERAD pathway
D	0042026	biological_process	protein refolding
D	0042149	biological_process	cellular response to glucose starvation
D	0042470	cellular_component	melanosome
D	0043022	molecular_function	ribosome binding
D	0043066	biological_process	negative regulation of apoptotic process
D	0043231	cellular_component	intracellular membrane-bounded organelle
D	0044183	molecular_function	protein folding chaperone
D	0045296	molecular_function	cadherin binding
D	0045944	biological_process	positive regulation of transcription by RNA polymerase II
D	0051082	molecular_function	unfolded protein binding
D	0051087	molecular_function	protein-folding chaperone binding
D	0051603	biological_process	proteolysis involved in protein catabolic process
D	0051787	molecular_function	misfolded protein binding
D	0060904	biological_process	regulation of protein folding in endoplasmic reticulum
D	0070062	cellular_component	extracellular exosome
D	0140311	molecular_function	protein sequestering activity
D	1903891	biological_process	regulation of ATF6-mediated unfolded protein response
D	1903894	biological_process	regulation of IRE1-mediated unfolded protein response
D	1903895	biological_process	negative regulation of IRE1-mediated unfolded protein response
D	1903897	biological_process	regulation of PERK-mediated unfolded protein response
D	1903898	biological_process	negative regulation of PERK-mediated unfolded protein response
E	0000166	molecular_function	nucleotide binding
E	0005509	molecular_function	calcium ion binding
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005634	cellular_component	nucleus
E	0005737	cellular_component	cytoplasm
E	0005739	cellular_component	mitochondrion
E	0005783	cellular_component	endoplasmic reticulum
E	0005788	cellular_component	endoplasmic reticulum lumen
E	0005789	cellular_component	endoplasmic reticulum membrane
E	0005793	cellular_component	endoplasmic reticulum-Golgi intermediate compartment
E	0005829	cellular_component	cytosol
E	0005886	cellular_component	plasma membrane
E	0005925	cellular_component	focal adhesion
E	0006457	biological_process	protein folding
E	0008180	cellular_component	COP9 signalosome
E	0009986	cellular_component	cell surface
E	0016020	cellular_component	membrane
E	0016787	molecular_function	hydrolase activity
E	0016887	molecular_function	ATP hydrolysis activity
E	0019899	molecular_function	enzyme binding
E	0019904	molecular_function	protein domain specific binding
E	0021589	biological_process	cerebellum structural organization
E	0021680	biological_process	cerebellar Purkinje cell layer development
E	0021762	biological_process	substantia nigra development
E	0030291	molecular_function	protein serine/threonine kinase inhibitor activity
E	0030335	biological_process	positive regulation of cell migration
E	0030496	cellular_component	midbody
E	0030968	biological_process	endoplasmic reticulum unfolded protein response
E	0031072	molecular_function	heat shock protein binding
E	0031204	biological_process	post-translational protein targeting to membrane, translocation
E	0031333	biological_process	negative regulation of protein-containing complex assembly
E	0031398	biological_process	positive regulation of protein ubiquitination
E	0031625	molecular_function	ubiquitin protein ligase binding
E	0032991	cellular_component	protein-containing complex
E	0034663	cellular_component	endoplasmic reticulum chaperone complex
E	0034975	biological_process	protein folding in endoplasmic reticulum
E	0034976	biological_process	response to endoplasmic reticulum stress
E	0035437	biological_process	maintenance of protein localization in endoplasmic reticulum
E	0036498	biological_process	IRE1-mediated unfolded protein response
E	0036503	biological_process	ERAD pathway
E	0042026	biological_process	protein refolding
E	0042149	biological_process	cellular response to glucose starvation
E	0042470	cellular_component	melanosome
E	0043022	molecular_function	ribosome binding
E	0043066	biological_process	negative regulation of apoptotic process
E	0043231	cellular_component	intracellular membrane-bounded organelle
E	0044183	molecular_function	protein folding chaperone
E	0045296	molecular_function	cadherin binding
E	0045944	biological_process	positive regulation of transcription by RNA polymerase II
E	0051082	molecular_function	unfolded protein binding
E	0051087	molecular_function	protein-folding chaperone binding
E	0051603	biological_process	proteolysis involved in protein catabolic process
E	0051787	molecular_function	misfolded protein binding
E	0060904	biological_process	regulation of protein folding in endoplasmic reticulum
E	0070062	cellular_component	extracellular exosome
E	0140311	molecular_function	protein sequestering activity
E	1903891	biological_process	regulation of ATF6-mediated unfolded protein response
E	1903894	biological_process	regulation of IRE1-mediated unfolded protein response
E	1903895	biological_process	negative regulation of IRE1-mediated unfolded protein response
E	1903897	biological_process	regulation of PERK-mediated unfolded protein response
E	1903898	biological_process	negative regulation of PERK-mediated unfolded protein response
F	0000166	molecular_function	nucleotide binding
F	0005509	molecular_function	calcium ion binding
F	0005515	molecular_function	protein binding
F	0005524	molecular_function	ATP binding
F	0005634	cellular_component	nucleus
F	0005737	cellular_component	cytoplasm
F	0005739	cellular_component	mitochondrion
F	0005783	cellular_component	endoplasmic reticulum
F	0005788	cellular_component	endoplasmic reticulum lumen
F	0005789	cellular_component	endoplasmic reticulum membrane
F	0005793	cellular_component	endoplasmic reticulum-Golgi intermediate compartment
F	0005829	cellular_component	cytosol
F	0005886	cellular_component	plasma membrane
F	0005925	cellular_component	focal adhesion
F	0006457	biological_process	protein folding
F	0008180	cellular_component	COP9 signalosome
F	0009986	cellular_component	cell surface
F	0016020	cellular_component	membrane
F	0016787	molecular_function	hydrolase activity
F	0016887	molecular_function	ATP hydrolysis activity
F	0019899	molecular_function	enzyme binding
F	0019904	molecular_function	protein domain specific binding
F	0021589	biological_process	cerebellum structural organization
F	0021680	biological_process	cerebellar Purkinje cell layer development
F	0021762	biological_process	substantia nigra development
F	0030291	molecular_function	protein serine/threonine kinase inhibitor activity
F	0030335	biological_process	positive regulation of cell migration
F	0030496	cellular_component	midbody
F	0030968	biological_process	endoplasmic reticulum unfolded protein response
F	0031072	molecular_function	heat shock protein binding
F	0031204	biological_process	post-translational protein targeting to membrane, translocation
F	0031333	biological_process	negative regulation of protein-containing complex assembly
F	0031398	biological_process	positive regulation of protein ubiquitination
F	0031625	molecular_function	ubiquitin protein ligase binding
F	0032991	cellular_component	protein-containing complex
F	0034663	cellular_component	endoplasmic reticulum chaperone complex
F	0034975	biological_process	protein folding in endoplasmic reticulum
F	0034976	biological_process	response to endoplasmic reticulum stress
F	0035437	biological_process	maintenance of protein localization in endoplasmic reticulum
F	0036498	biological_process	IRE1-mediated unfolded protein response
F	0036503	biological_process	ERAD pathway
F	0042026	biological_process	protein refolding
F	0042149	biological_process	cellular response to glucose starvation
F	0042470	cellular_component	melanosome
F	0043022	molecular_function	ribosome binding
F	0043066	biological_process	negative regulation of apoptotic process
F	0043231	cellular_component	intracellular membrane-bounded organelle
F	0044183	molecular_function	protein folding chaperone
F	0045296	molecular_function	cadherin binding
F	0045944	biological_process	positive regulation of transcription by RNA polymerase II
F	0051082	molecular_function	unfolded protein binding
F	0051087	molecular_function	protein-folding chaperone binding
F	0051603	biological_process	proteolysis involved in protein catabolic process
F	0051787	molecular_function	misfolded protein binding
F	0060904	biological_process	regulation of protein folding in endoplasmic reticulum
F	0070062	cellular_component	extracellular exosome
F	0140311	molecular_function	protein sequestering activity
F	1903891	biological_process	regulation of ATF6-mediated unfolded protein response
F	1903894	biological_process	regulation of IRE1-mediated unfolded protein response
F	1903895	biological_process	negative regulation of IRE1-mediated unfolded protein response
F	1903897	biological_process	regulation of PERK-mediated unfolded protein response
F	1903898	biological_process	negative regulation of PERK-mediated unfolded protein response

Functional Information from PDB Data

site_id	AC1
Number of Residues	21
Details	binding site for residue ATP A 801

Chain	Residue
A	GLY36
A	ALA229
A	GLY255
A	GLU293
A	LYS296
A	ARG297
A	SER300
A	GLY363
A	GLY364
A	SER365
A	ARG367
A	THR37
A	ILE368
A	ZN802
A	THR38
A	TYR39
A	LYS96
A	GLU201
A	GLY226
A	GLY227
A	GLY228

---

site_id	AC2
Number of Residues	2
Details	binding site for residue ZN A 802

Chain	Residue
A	ASP34
A	ATP801

---

site_id	AC3
Number of Residues	5
Details	binding site for residue MG A 803

Chain	Residue
A	ASP608
A	ASP611
C	ASP608
C	ASP611
C	MG803

---

site_id	AC4
Number of Residues	3
Details	binding site for residue MG A 804

Chain	Residue
A	GLU316
C	GLU310
C	ASP317

---

site_id	AC5
Number of Residues	3
Details	binding site for residue MG A 805

Chain	Residue
A	GLU310
A	ASP317
C	GLU316

---

site_id	AC6
Number of Residues	3
Details	binding site for residue ZN A 806

Chain	Residue
A	GLU201
A	ASP224
A	ASP231

---

site_id	AC7
Number of Residues	1
Details	binding site for residue ZN A 807

Chain	Residue
A	ASP238

---

site_id	AC8
Number of Residues	4
Details	binding site for residue SO4 A 808

Chain	Residue
A	GLU25
A	VAL27
A	HIS167
A	ASN194

---

site_id	AC9
Number of Residues	24
Details	binding site for residue ATP B 801

Chain	Residue
B	ASP34
B	GLY36
B	THR37
B	THR38
B	TYR39
B	LYS96
B	GLU201
B	GLY226
B	GLY227
B	GLY228
B	ALA229
B	GLY255
B	GLU293
B	LYS296
B	ARG297
B	SER300
B	GLY363
B	GLY364
B	SER365
B	ARG367
B	ILE368
B	ZN802
B	ZN803
B	HOH903

---

site_id	AD1
Number of Residues	3
Details	binding site for residue ZN B 802

Chain	Residue
B	ASP34
B	ATP801
B	HOH903

---

site_id	AD2
Number of Residues	5
Details	binding site for residue ZN B 803

Chain	Residue
B	GLU201
B	ASP224
B	ALA229
B	ASP231
B	ATP801

---

site_id	AD3
Number of Residues	3
Details	binding site for residue MG B 804

Chain	Residue
B	ASP608
B	ASP611
D	ASP606

---

site_id	AD4
Number of Residues	3
Details	binding site for residue MG B 805

Chain	Residue
B	GLU310
B	ASP317
F	GLU314

---

site_id	AD5
Number of Residues	2
Details	binding site for residue MG B 806

Chain	Residue
B	GLU316
F	GLU316

---

site_id	AD6
Number of Residues	1
Details	binding site for residue ZN B 807

Chain	Residue
B	ASP238

---

site_id	AD7
Number of Residues	3
Details	binding site for residue SO4 B 808

Chain	Residue
B	GLU25
B	HIS167
B	ASN194

---

site_id	AD8
Number of Residues	23
Details	binding site for residue ATP C 801

Chain	Residue
C	ARG297
C	SER300
C	GLY363
C	GLY364
C	SER365
C	ARG367
C	ILE368
C	ASP391
C	ZN802
C	HOH901
C	GLY36
C	THR37
C	THR38
C	TYR39
C	LYS96
C	GLU201
C	GLY226
C	GLY227
C	GLY228
C	ALA229
C	GLY255
C	GLU293
C	LYS296

---

site_id	AD9
Number of Residues	3
Details	binding site for residue ZN C 802

Chain	Residue
C	ASP34
C	ATP801
C	HOH901

---

site_id	AE1
Number of Residues	5
Details	binding site for residue MG C 803

Chain	Residue
A	ASP608
A	ASP611
A	MG803
C	ASP608
C	ASP611

---

site_id	AE2
Number of Residues	3
Details	binding site for residue ZN C 804

Chain	Residue
C	GLU201
C	ASP224
C	ASP231

---

site_id	AE3
Number of Residues	1
Details	binding site for residue ZN C 805

Chain	Residue
C	ASP238

---

site_id	AE4
Number of Residues	4
Details	binding site for residue SO4 C 806

Chain	Residue
C	GLU25
C	VAL27
C	HIS167
C	ASN194

---

site_id	AE5
Number of Residues	22
Details	binding site for residue ATP D 801

Chain	Residue
D	GLY36
D	THR37
D	THR38
D	TYR39
D	LYS96
D	GLU201
D	GLY226
D	GLY227
D	GLY228
D	ALA229
D	GLY255
D	GLU293
D	LYS296
D	ARG297
D	SER300
D	GLY363
D	GLY364
D	SER365
D	ARG367
D	ILE368
D	ZN802
D	HOH901

---

site_id	AE6
Number of Residues	3
Details	binding site for residue ZN D 802

Chain	Residue
D	ASP34
D	ATP801
D	HOH901

---

site_id	AE7
Number of Residues	3
Details	binding site for residue MG D 803

Chain	Residue
B	LYS550
D	ASP608
D	ASP611

---

site_id	AE8
Number of Residues	3
Details	binding site for residue MG D 804

Chain	Residue
D	GLU316
E	GLU310
E	ASP317

---

site_id	AE9
Number of Residues	3
Details	binding site for residue MG D 805

Chain	Residue
D	GLU310
D	ASP317
E	GLU316

---

site_id	AF1
Number of Residues	3
Details	binding site for residue ZN D 806

Chain	Residue
D	GLU201
D	ASP224
D	ASP231

---

site_id	AF2
Number of Residues	1
Details	binding site for residue ZN D 807

Chain	Residue
D	ASP238

---

site_id	AF3
Number of Residues	4
Details	binding site for residue SO4 D 808

Chain	Residue
D	GLU25
D	VAL27
D	HIS167
D	ASN194

---

site_id	AF4
Number of Residues	24
Details	binding site for residue ATP E 801

Chain	Residue
E	GLY36
E	THR37
E	THR38
E	TYR39
E	LYS96
E	GLU201
E	GLY226
E	GLY227
E	GLY228
E	ALA229
E	GLY255
E	GLU293
E	LYS296
E	ARG297
E	SER300
E	GLY363
E	GLY364
E	SER365
E	ARG367
E	ILE368
E	ASP391
E	ZN803
E	ZN804
E	HOH903

---

site_id	AF5
Number of Residues	3
Details	binding site for residue MG E 802

Chain	Residue
E	ASP608
E	ASP611
F	LYS550

---

site_id	AF6
Number of Residues	4
Details	binding site for residue ZN E 803

Chain	Residue
E	GLU201
E	ASP224
E	ASP231
E	ATP801

---

site_id	AF7
Number of Residues	3
Details	binding site for residue ZN E 804

Chain	Residue
E	ASP34
E	ATP801
E	HOH903

---

site_id	AF8
Number of Residues	1
Details	binding site for residue ZN E 805

Chain	Residue
E	ASP238

---

site_id	AF9
Number of Residues	3
Details	binding site for residue SO4 E 806

Chain	Residue
E	GLU25
E	HIS167
E	ASN194

---

site_id	AG1
Number of Residues	23
Details	binding site for residue ATP F 801

Chain	Residue
F	ASP34
F	GLY36
F	THR37
F	THR38
F	TYR39
F	LYS96
F	GLU201
F	GLY226
F	GLY227
F	GLY228
F	ALA229
F	GLY255
F	GLU293
F	LYS296
F	ARG297
F	SER300
F	GLY363
F	GLY364
F	SER365
F	ARG367
F	ILE368
F	ZN802
F	HOH901

---

site_id	AG2
Number of Residues	3
Details	binding site for residue ZN F 802

Chain	Residue
F	ASP34
F	ATP801
F	HOH901

---

site_id	AG3
Number of Residues	3
Details	binding site for residue MG F 803

Chain	Residue
E	ASP606
F	ASP608
F	ASP611

---

site_id	AG4
Number of Residues	3
Details	binding site for residue ZN F 804

Chain	Residue
F	GLU201
F	ASP224
F	ASP231

---

site_id	AG5
Number of Residues	1
Details	binding site for residue ZN F 805

Chain	Residue
F	ASP238

---

site_id	AG6
Number of Residues	4
Details	binding site for residue SO4 F 806

Chain	Residue
F	GLU25
F	VAL27
F	HIS167
F	ASN194

---

Functional Information from PROSITE/UniProt

site_id	PS00297
Number of Residues	8
Details	HSP70_1 Heat shock hsp70 proteins family signature 1. IDLGTTyS

Chain	Residue	Details
A	ILE33-SER40

---

site_id	PS00329
Number of Residues	14
Details	HSP70_2 Heat shock hsp70 proteins family signature 2. VFDLGGGAfdvSLL

Chain	Residue	Details
A	VAL222-LEU235

---

site_id	PS01036
Number of Residues	15
Details	HSP70_3 Heat shock hsp70 proteins family signature 3. IvLvGGsTRIPkIqQ

Chain	Residue	Details
A	ILE359-GLN373

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	930
Details	Region: {"description":"Nucleotide-binding (NBD)","evidences":[{"source":"PubMed","id":"28286085","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	60
Details	Region: {"description":"Interdomain linker","evidences":[{"source":"UniProtKB","id":"G3I8R9","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	96
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21526763","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P06761","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	18
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P20029","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	6
Details	Modified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"UniProtKB","id":"P20029","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	6
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P0DMV8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	6
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P20029","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	6
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P20029","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	6
Details	Modified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"UniProtKB","id":"P0DMV8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	6
Details	Modified residue: {"description":"Phosphothreonine; alternate","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
Number of Residues	6
Details	Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"24129315","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI13
Number of Residues	6
Details	Modified residue: {"description":"N6-methyllysine","evidences":[{"source":"PubMed","id":"24129315","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI14
Number of Residues	6
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"25114211","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25218447","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25755297","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI15
Number of Residues	12
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate","evidences":[{"source":"PubMed","id":"25114211","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---