6BYF

Crystal structure of the core catalytic domain of PP-IP phosphatase SIW14 from S. cerevisiae in complex with citrate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006470	biological_process	protein dephosphorylation
A	0016311	biological_process	dephosphorylation
A	0016791	molecular_function	phosphatase activity
B	0006470	biological_process	protein dephosphorylation
B	0016311	biological_process	dephosphorylation
B	0016791	molecular_function	phosphatase activity
C	0006470	biological_process	protein dephosphorylation
C	0016311	biological_process	dephosphorylation
C	0016791	molecular_function	phosphatase activity
D	0006470	biological_process	protein dephosphorylation
D	0016311	biological_process	dephosphorylation
D	0016791	molecular_function	phosphatase activity
E	0006470	biological_process	protein dephosphorylation
E	0016311	biological_process	dephosphorylation
E	0016791	molecular_function	phosphatase activity
F	0006470	biological_process	protein dephosphorylation
F	0016311	biological_process	dephosphorylation
F	0016791	molecular_function	phosphatase activity
G	0006470	biological_process	protein dephosphorylation
G	0016311	biological_process	dephosphorylation
G	0016791	molecular_function	phosphatase activity
H	0006470	biological_process	protein dephosphorylation
H	0016311	biological_process	dephosphorylation
H	0016791	molecular_function	phosphatase activity
I	0006470	biological_process	protein dephosphorylation
I	0016311	biological_process	dephosphorylation
I	0016791	molecular_function	phosphatase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	binding site for residue CIT A 301

Chain	Residue
A	CYS214
A	HOH415
A	ASN215
A	ARG216
A	GLY217
A	LYS218
A	HIS219
A	ARG220
A	LYS250
A	HOH402

---

site_id	AC2
Number of Residues	5
Details	binding site for residue EDO A 302

Chain	Residue
A	MSE238
A	ASP241
A	ARG245
E	ASN121
E	PHE122

---

site_id	AC3
Number of Residues	10
Details	binding site for residue CIT B 301

Chain	Residue
B	CYS214
B	ASN215
B	ARG216
B	GLY217
B	LYS218
B	HIS219
B	ARG220
B	LYS250
B	HOH407
B	HOH409

---

site_id	AC4
Number of Residues	9
Details	binding site for residue CIT C 301

Chain	Residue
C	ASN183
C	CYS214
C	ASN215
C	ARG216
C	GLY217
C	LYS218
C	HIS219
C	ARG220
C	LYS250

---

site_id	AC5
Number of Residues	5
Details	binding site for residue EDO C 302

Chain	Residue
C	MSE238
C	ASP241
C	ARG245
D	ASN121
D	PHE122

---

site_id	AC6
Number of Residues	7
Details	binding site for residue CIT D 301

Chain	Residue
D	CYS214
D	ASN215
D	ARG216
D	LYS218
D	HIS219
D	ARG220
D	HOH404

---

site_id	AC7
Number of Residues	5
Details	binding site for residue EDO D 302

Chain	Residue
C	ASN121
C	PHE122
D	MSE238
D	ASP241
D	ARG245

---

site_id	AC8
Number of Residues	4
Details	binding site for residue CL D 303

Chain	Residue
C	ARG146
D	GLN232
D	TRP234
D	TRP281

---

site_id	AC9
Number of Residues	10
Details	binding site for residue CIT E 301

Chain	Residue
E	CYS214
E	ASN215
E	ARG216
E	GLY217
E	LYS218
E	HIS219
E	ARG220
E	LYS250
E	HOH407
E	HOH431

---

site_id	AD1
Number of Residues	9
Details	binding site for residue CIT F 301

Chain	Residue
F	CYS214
F	ASN215
F	ARG216
F	GLY217
F	LYS218
F	HIS219
F	ARG220
F	LYS250
F	HOH401

---

site_id	AD2
Number of Residues	8
Details	binding site for residue CIT G 301

Chain	Residue
G	CYS214
G	ASN215
G	ARG216
G	GLY217
G	LYS218
G	HIS219
G	ARG220
G	LYS250

---

site_id	AD3
Number of Residues	5
Details	binding site for residue CL G 302

Chain	Residue
G	PHE142
G	ARG146
H	GLN232
H	TRP234
H	TRP281

---

site_id	AD4
Number of Residues	9
Details	binding site for residue CIT H 301

Chain	Residue
H	CYS214
H	ASN215
H	ARG216
H	GLY217
H	LYS218
H	HIS219
H	ARG220
H	LYS250
H	HOH412

---

site_id	AD5
Number of Residues	9
Details	binding site for residue CIT I 301

Chain	Residue
I	GLY217
I	LYS218
I	HIS219
I	ARG220
I	HOH405
I	HOH407
I	CYS214
I	ASN215
I	ARG216

---

Functional Information from PROSITE/UniProt

site_id	PS00383
Number of Residues	11
Details	TYR_PHOSPHATASE_1 Tyrosine specific protein phosphatases active site. IHCnrGkhRTG

Chain	Residue	Details
A	ILE212-GLY222

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	9
Details	ACT_SITE: Phosphocysteine intermediate => ECO:0000255|PROSITE-ProRule:PRU00160, ECO:0000305|PubMed:29540476

Chain	Residue	Details
A	CYS214
B	CYS214
C	CYS214
D	CYS214
E	CYS214
F	CYS214
G	CYS214
H	CYS214
I	CYS214

---

site_id	SWS_FT_FI2
Number of Residues	27
Details	BINDING: BINDING => ECO:0000250|UniProtKB:Q9ZVN4

Chain	Residue	Details
A	ASN189
D	ASN189
D	ILE190
D	HIS193
E	ASN189
E	ILE190
E	HIS193
F	ASN189
F	ILE190
F	HIS193
G	ASN189
A	ILE190
G	ILE190
G	HIS193
H	ASN189
H	ILE190
H	HIS193
I	ASN189
I	ILE190
I	HIS193
A	HIS193
B	ASN189
B	ILE190
B	HIS193
C	ASN189
C	ILE190
C	HIS193

---

site_id	SWS_FT_FI3
Number of Residues	9
Details	SITE: Transition state stabilizer => ECO:0000305|PubMed:29540476

Chain	Residue	Details
A	ARG220
B	ARG220
C	ARG220
D	ARG220
E	ARG220
F	ARG220
G	ARG220
H	ARG220
I	ARG220

---