5D4W

Crystal structure of Hsp104

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006457	biological_process	protein folding
A	0016887	molecular_function	ATP hydrolysis activity
A	0034605	biological_process	cellular response to heat
A	0042026	biological_process	protein refolding
A	0043335	biological_process	protein unfolding
A	0051082	molecular_function	unfolded protein binding
A	0051087	molecular_function	protein-folding chaperone binding
A	0070370	biological_process	cellular heat acclimation
B	0000166	molecular_function	nucleotide binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006457	biological_process	protein folding
B	0016887	molecular_function	ATP hydrolysis activity
B	0034605	biological_process	cellular response to heat
B	0042026	biological_process	protein refolding
B	0043335	biological_process	protein unfolding
B	0051082	molecular_function	unfolded protein binding
B	0051087	molecular_function	protein-folding chaperone binding
B	0070370	biological_process	cellular heat acclimation
C	0000166	molecular_function	nucleotide binding
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006457	biological_process	protein folding
C	0016887	molecular_function	ATP hydrolysis activity
C	0034605	biological_process	cellular response to heat
C	0042026	biological_process	protein refolding
C	0043335	biological_process	protein unfolding
C	0051082	molecular_function	unfolded protein binding
C	0051087	molecular_function	protein-folding chaperone binding
C	0070370	biological_process	cellular heat acclimation

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	binding site for residue ADP A 1001

Chain	Residue
A	VAL197
A	LYS229
A	THR230
A	THR231
A	ILE367
A	LEU371
A	TYR375
A	ASP406
A	VAL409
B	ARG349
A	ILE198
A	GLY199
A	ARG200
A	GLU224
A	PRO225
A	GLY226
A	VAL227
A	GLY228

---

site_id	AC2
Number of Residues	10
Details	binding site for residue ADP A 1002

Chain	Residue
A	VAL600
A	SER636
A	THR638
A	GLY639
A	LYS640
A	THR641
A	LEU642
A	ASP706
A	ILE806
B	ARG788

---

site_id	AC3
Number of Residues	18
Details	binding site for residue ADP B 1001

Chain	Residue
B	VAL197
B	ILE198
B	GLY199
B	ARG200
B	GLU224
B	PRO225
B	GLY226
B	VAL227
B	GLY228
B	LYS229
B	THR230
B	THR231
B	ILE367
B	LEU371
B	TYR375
B	ASP406
B	VAL409
C	ARG349

---

site_id	AC4
Number of Residues	10
Details	binding site for residue ADP B 1002

Chain	Residue
B	VAL600
B	VAL601
B	THR638
B	GLY639
B	LYS640
B	THR641
B	LEU642
B	ILE806
B	ARG849
C	ARG788

---

site_id	AC5
Number of Residues	18
Details	binding site for residue ADP C 1001

Chain	Residue
C	VAL197
C	ILE198
C	GLY199
C	ARG200
C	GLU224
C	PRO225
C	GLY226
C	VAL227
C	GLY228
C	LYS229
C	THR230
C	THR231
C	ILE367
C	LEU371
C	TYR375
C	PRO405
C	ASP406
C	VAL409

---

site_id	AC6
Number of Residues	10
Details	binding site for residue ADP C 1002

Chain	Residue
C	VAL600
C	VAL601
C	THR638
C	GLY639
C	LYS640
C	THR641
C	LEU642
C	ILE806
C	ARG810
C	ALA848

---

Functional Information from PROSITE/UniProt

site_id	PS00870
Number of Residues	13
Details	CLPAB_1 Chaperonins clpA/B signature 1. DAANLLKPmLarG

Chain	Residue	Details
A	ASP312-GLY324

---

site_id	PS00871
Number of Residues	19
Details	CLPAB_2 Chaperonins clpA/B signature 2. RFDmSEYqERhSlSRMiGA

Chain	Residue	Details
A	ARG660-ALA678

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