5ZR3

Crystal structure of Hsp90-alpha N-terminal domain in complex with 4-(3-isopropyl-4-(4-(1-methyl-1H-pyrazol-4-yl)-1H-imidazol-1-yl)-1H-pyrazolo[3,4-b]pyridin-1-yl)-3-methylbenzamide

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
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
E	0005524	molecular_function	ATP binding
E	0006457	biological_process	protein folding
E	0016887	molecular_function	ATP hydrolysis activity
E	0051082	molecular_function	unfolded protein binding
E	0140662	molecular_function	ATP-dependent protein folding chaperone
G	0005524	molecular_function	ATP binding
G	0006457	biological_process	protein folding
G	0016887	molecular_function	ATP hydrolysis activity
G	0051082	molecular_function	unfolded protein binding
G	0140662	molecular_function	ATP-dependent protein folding chaperone

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	binding site for residue 9J0 A 301

Chain	Residue
A	PHE22
A	TYR139
A	TRP162
A	PHE170
A	THR184
A	HOH412
A	HOH429
A	ALA55
A	ASP93
A	MET98
A	LEU103
A	ILE104
A	GLY108
A	GLY135
A	PHE138

---

site_id	AC2
Number of Residues	14
Details	binding site for residue 9J0 C 301

Chain	Residue
C	SER52
C	ALA55
C	ASP93
C	MET98
C	LEU103
C	ILE104
C	GLY108
C	GLY135
C	PHE138
C	TYR139
C	TRP162
C	PHE170
C	HOH404
C	HOH411

---

site_id	AC3
Number of Residues	16
Details	binding site for residue 9J0 E 301

Chain	Residue
E	PHE22
E	SER52
E	ALA55
E	ASP93
E	MET98
E	LEU103
E	ILE104
E	GLY108
E	GLY135
E	PHE138
E	TYR139
E	TRP162
E	PHE170
E	HOH401
E	HOH406
E	HOH411

---

site_id	AC4
Number of Residues	16
Details	binding site for residue 9J0 G 301

Chain	Residue
G	PHE22
G	SER52
G	ALA55
G	ASP93
G	MET98
G	LEU103
G	ILE104
G	GLY108
G	PHE138
G	TYR139
G	TRP162
G	PHE170
G	THR184
G	HOH406
G	HOH422
G	HOH423

---

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	TYR38-GLU47

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	BINDING:

Chain	Residue	Details
A	ASN51
G	ASN51
G	ASP93
G	PHE138
A	ASP93
A	PHE138
C	ASN51
C	ASP93
C	PHE138
E	ASN51
E	ASP93
E	PHE138

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	LYS112
C	LYS112
E	LYS112
G	LYS112

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	MOD_RES: Phosphothreonine; by PRKDC => ECO:0000269|PubMed:2507541

Chain	Residue	Details
A	THR5
A	THR7
C	THR5
C	THR7
E	THR5
E	THR7
G	THR5
G	THR7

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P07901

Chain	Residue	Details
A	LYS58
A	LYS84
C	LYS58
C	LYS84
E	LYS58
E	LYS84
G	LYS58
G	LYS84

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:2492519, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	SER231
C	SER231
E	SER231
G	SER231

---