5UCI

Hsp90b N-terminal domain with inhibitors

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005524	molecular_function	ATP binding
A	0006457	biological_process	protein folding
A	0016887	molecular_function	ATP hydrolysis activity
A	0051082	molecular_function	unfolded protein binding
A	0140662	molecular_function	ATP-dependent protein folding chaperone
B	0005524	molecular_function	ATP binding
B	0006457	biological_process	protein folding
B	0016887	molecular_function	ATP hydrolysis activity
B	0051082	molecular_function	unfolded protein binding
B	0140662	molecular_function	ATP-dependent protein folding chaperone
C	0005524	molecular_function	ATP binding
C	0006457	biological_process	protein folding
C	0016887	molecular_function	ATP hydrolysis activity
C	0051082	molecular_function	unfolded protein binding
C	0140662	molecular_function	ATP-dependent protein folding chaperone
D	0005524	molecular_function	ATP binding
D	0006457	biological_process	protein folding
D	0016887	molecular_function	ATP hydrolysis activity
D	0051082	molecular_function	unfolded protein binding
D	0140662	molecular_function	ATP-dependent protein folding chaperone

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	binding site for residue 874 A 301

Chain	Residue
A	LEU43
A	PHE133
A	THR179
A	VAL181
A	DMS302
A	ASN46
A	ALA47
A	ASP49
A	ALA50
A	LEU86
A	ASP88
A	GLY92
A	MET93

---

site_id	AC2
Number of Residues	3
Details	binding site for residue DMS A 302

Chain	Residue
A	ASN101
A	GLY130
A	874301

---

site_id	AC3
Number of Residues	12
Details	binding site for residue 874 B 301

Chain	Residue
B	LEU43
B	ASN46
B	ALA47
B	ASP49
B	ALA50
B	ASP88
B	ILE91
B	MET93
B	PHE133
B	THR179
B	VAL181
B	DMS302

---

site_id	AC4
Number of Residues	4
Details	binding site for residue DMS B 302

Chain	Residue
B	ASN101
B	ALA106
B	GLY130
B	874301

---

site_id	AC5
Number of Residues	6
Details	binding site for residue GOL B 303

Chain	Residue
B	ALA16
B	PHE17
B	ALA19
C	PHE17
C	GLN18
C	ALA19

---

site_id	AC6
Number of Residues	13
Details	binding site for residue 874 C 301

Chain	Residue
C	LEU43
C	ASN46
C	ALA47
C	ALA50
C	LYS53
C	LEU86
C	ASP88
C	ILE91
C	MET93
C	PHE133
C	THR179
C	VAL181
C	DMS302

---

site_id	AC7
Number of Residues	4
Details	binding site for residue DMS C 302

Chain	Residue
C	ASN101
C	GLY130
C	TYR134
C	874301

---

site_id	AC8
Number of Residues	12
Details	binding site for residue 874 D 301

Chain	Residue
D	LEU43
D	ASN46
D	ALA47
D	ALA50
D	LYS53
D	ASP88
D	MET93
D	LEU102
D	PHE133
D	THR179
D	VAL181
D	HOH405

---

site_id	AC9
Number of Residues	6
Details	binding site for residue GOL D 302

Chain	Residue
A	ALA16
A	PHE17
A	ALA19
D	PHE17
D	GLN18
D	ALA19

---

site_id	AD1
Number of Residues	3
Details	binding site for residue DMS D 303

Chain	Residue
D	ASN101
D	GLY130
D	TYR134

---

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	TYR33-GLU42

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	ASN46
D	ASN46
D	LYS107
D	PHE133
A	LYS107
A	PHE133
B	ASN46
B	LYS107
B	PHE133
C	ASN46
C	LYS107
C	PHE133

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING:

Chain	Residue	Details
A	ASP88
B	ASP88
C	ASP88
D	ASP88

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	SITE: Cleaved under oxidative stress => ECO:0000269|PubMed:22848402

Chain	Residue	Details
A	ILE126
B	ILE126
C	ILE126
D	ILE126

---