6XLH

Asymmetric hydrolysis state of Hsc82 in complex with Aha1 bound with ADP and ATPgammaS

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000492	biological_process	box C/D snoRNP assembly
A	0000723	biological_process	telomere maintenance
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006457	biological_process	protein folding
A	0016887	molecular_function	ATP hydrolysis activity
A	0032991	cellular_component	protein-containing complex
A	0034605	biological_process	cellular response to heat
A	0043248	biological_process	proteasome assembly
A	0048471	cellular_component	perinuclear region of cytoplasm
A	0050821	biological_process	protein stabilization
A	0051082	molecular_function	unfolded protein binding
A	0070482	biological_process	response to oxygen levels
A	0140662	molecular_function	ATP-dependent protein folding chaperone
B	0000166	molecular_function	nucleotide binding
B	0000492	biological_process	box C/D snoRNP assembly
B	0000723	biological_process	telomere maintenance
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005739	cellular_component	mitochondrion
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0006457	biological_process	protein folding
B	0016887	molecular_function	ATP hydrolysis activity
B	0032991	cellular_component	protein-containing complex
B	0034605	biological_process	cellular response to heat
B	0043248	biological_process	proteasome assembly
B	0048471	cellular_component	perinuclear region of cytoplasm
B	0050821	biological_process	protein stabilization
B	0051082	molecular_function	unfolded protein binding
B	0070482	biological_process	response to oxygen levels
B	0140662	molecular_function	ATP-dependent protein folding chaperone
C	0001671	molecular_function	ATPase activator activity
C	0005515	molecular_function	protein binding
C	0005634	cellular_component	nucleus
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006457	biological_process	protein folding
C	0006606	biological_process	protein import into nucleus
C	0051087	molecular_function	protein-folding chaperone binding
D	0001671	molecular_function	ATPase activator activity
D	0005515	molecular_function	protein binding
D	0005634	cellular_component	nucleus
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006457	biological_process	protein folding
D	0006606	biological_process	protein import into nucleus
D	0051087	molecular_function	protein-folding chaperone binding

Functional Information from PDB Data

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

Chain	Residue
A	ASN37
A	ILE117
A	GLY118
A	GLN119
A	PHE120
A	GLY121
A	VAL122
A	GLY123
A	PHE124
A	THR171
A	ARG376
A	ALA41
A	MG802
A	K803
A	LYS44
A	ASP79
A	MET84
A	ASN92
A	SER99
A	GLY100
A	THR101

---

site_id	AC2
Number of Residues	3
Details	binding site for residue MG A 802

Chain	Residue
A	GLU33
A	ASN37
A	AGS801

---

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

Chain	Residue
A	ASN92
A	THR95
A	LYS98
A	GLY121
A	AGS801

---

site_id	AC4
Number of Residues	18
Details	binding site for residue ADP B 801

Chain	Residue
B	ASN37
B	ALA41
B	LYS44
B	ASP79
B	MET84
B	SER99
B	GLY100
B	THR101
B	GLY118
B	GLN119
B	PHE120
B	GLY121
B	VAL122
B	GLY123
B	PHE124
B	THR171
B	MG802
B	K803

---

site_id	AC5
Number of Residues	3
Details	binding site for residue MG B 802

Chain	Residue
B	GLU33
B	ASN37
B	ADP801

---

site_id	AC6
Number of Residues	5
Details	binding site for residue K B 803

Chain	Residue
B	ASN92
B	THR95
B	LYS98
B	GLY121
B	ADP801

---

Functional Information from PROSITE/UniProt

site_id	PS00298
Number of Residues	10
Details	HSP90 Heat shock hsp90 proteins family signature. YsNKEIFLRE

Chain	Residue	Details
A	TYR24-GLU33

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	10
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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