5BZX

Crystal structure of human phosphatase PTEN treated with a bisperoxovanadium complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016311	biological_process	dephosphorylation
A	0016791	molecular_function	phosphatase activity
B	0016311	biological_process	dephosphorylation
B	0016791	molecular_function	phosphatase activity
C	0016311	biological_process	dephosphorylation
C	0016791	molecular_function	phosphatase activity
D	0016311	biological_process	dephosphorylation
D	0016791	molecular_function	phosphatase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	binding site for residue VO4 A 401

Chain	Residue
A	CYS124
A	HOH563
A	LYS125
A	ALA126
A	GLY127
A	LYS128
A	GLY129
A	ARG130
A	THR131
A	HOH507

---

site_id	AC2
Number of Residues	13
Details	binding site for residue TLA B 401

Chain	Residue
B	ASP92
B	HIS93
B	CYS124
B	LYS125
B	ALA126
B	GLY127
B	LYS128
B	GLY129
B	ARG130
B	THR131
B	HOH502
B	HOH503
B	HOH521

---

site_id	AC3
Number of Residues	13
Details	binding site for residue TLA D 401

Chain	Residue
D	ASP92
D	HIS93
D	CYS124
D	LYS125
D	ALA126
D	GLY127
D	LYS128
D	GLY129
D	ARG130
D	THR131
D	HOH502
D	HOH510
D	HOH521

---

site_id	AC4
Number of Residues	12
Details	binding site for residues TLA C 401 and VO4 C 402

Chain	Residue
C	ASP92
C	HIS93
C	CYS124
C	LYS125
C	ALA126
C	GLY127
C	LYS128
C	GLY129
C	ARG130
C	THR131
C	GLN171
C	HOH542

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE122-GLY132

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	684
Details	Domain: {"description":"Phosphatase tensin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00590","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	40
Details	Region: {"description":"Required for interaction with NOP53","evidences":[{"source":"PubMed","id":"15355975","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Active site: {"description":"Phosphocysteine intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00590","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"26166433","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Modified residue: {"description":"Phosphotyrosine; by FRK","evidences":[{"source":"PubMed","id":"19345329","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	3
Details	M-CSA 456

Chain	Residue	Details
A	ASP92	proton shuttle (general acid/base)
A	CYS124	covalent catalysis
A	ARG130	transition state stabiliser

---

site_id	MCSA2
Number of Residues	3
Details	M-CSA 456

Chain	Residue	Details
B	ASP92	proton shuttle (general acid/base)
B	CYS124	covalent catalysis
B	ARG130	transition state stabiliser

---

site_id	MCSA3
Number of Residues	3
Details	M-CSA 456

Chain	Residue	Details
C	ASP92	proton shuttle (general acid/base)
C	CYS124	covalent catalysis
C	ARG130	transition state stabiliser

---

site_id	MCSA4
Number of Residues	3
Details	M-CSA 456

Chain	Residue	Details
D	ASP92	proton shuttle (general acid/base)
D	CYS124	covalent catalysis
D	ARG130	transition state stabiliser

---