3PRY

Crystal structure of the middle domain of human HSP90-beta refined at 2.3 A resolution

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 1

Chain	Residue
A	HOH203
A	LYS411
A	LYS538
A	GLU539
A	GLY540

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 3

Chain	Residue
B	GLY540
B	HOH185
B	LYS411
B	LYS538
B	GLU539

---

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL B 4

Chain	Residue
B	VAL318
B	LYS319
B	HIS320

---

site_id	AC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE EDO B 5

Chain	Residue
B	ARG506

---

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO B 6

Chain	Residue
B	ILE370
B	GLU372
B	ARG405

---

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO B 7

Chain	Residue
B	VAL403
B	ASN407
B	LYS410
B	GLU539
B	LEU541
B	GLU542

---

site_id	AC7
Number of Residues	1
Details	BINDING SITE FOR RESIDUE EDO B 8

Chain	Residue
B	GLU443

---

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO C 9

Chain	Residue
C	SER434
C	MET466

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	ARG392
B	ARG392
C	ARG392

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:17525332, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	THR297
B	THR297
C	THR297

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	MOD_RES: Phosphotyrosine; by SRC => ECO:0000269|PubMed:23585225

Chain	Residue	Details
A	TYR301
B	TYR301
C	TYR301

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P11499

Chain	Residue	Details
A	TYR305
A	TYR484
B	TYR305
B	TYR484
C	TYR305
C	TYR484

---

site_id	SWS_FT_FI5
Number of Residues	3
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648

Chain	Residue	Details
A	SER307
B	SER307
C	SER307

---

site_id	SWS_FT_FI6
Number of Residues	3
Details	MOD_RES: N6-malonyllysine => ECO:0000269|PubMed:21908771

Chain	Residue	Details
A	LYS399
B	LYS399
C	LYS399

---

site_id	SWS_FT_FI7
Number of Residues	6
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861

Chain	Residue	Details
A	LYS435
A	LYS481
B	LYS435
B	LYS481
C	LYS435
C	LYS481

---

site_id	SWS_FT_FI8
Number of Residues	3
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER445
B	SER445
C	SER445

---

site_id	SWS_FT_FI9
Number of Residues	3
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	THR479
B	THR479
C	THR479

---

site_id	SWS_FT_FI10
Number of Residues	3
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P11499

Chain	Residue	Details
A	LYS531
B	LYS531
C	LYS531

---

site_id	SWS_FT_FI11
Number of Residues	6
Details	CARBOHYD: O-linked (GlcNAc) serine => ECO:0000250

Chain	Residue	Details
A	SER434
A	SER452
B	SER434
B	SER452
C	SER434
C	SER452

---