3H63

Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c) with two Mn2+ atoms originally soaked with cantharidin (which is present in the structure in the hydrolyzed form)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016787	molecular_function	hydrolase activity
C	0016787	molecular_function	hydrolase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MN A 500

Chain	Residue
A	NHC1
A	ASP271
A	ASN303
A	HIS352
A	HIS427
A	MN501
A	HOH871

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN A 501

Chain	Residue
A	HIS244
A	ASP271
A	MN500
A	NHC1
A	ASP242

---

site_id	AC3
Number of Residues	17
Details	BINDING SITE FOR RESIDUE NHC A 1

Chain	Residue
A	ASP242
A	HIS244
A	ASP271
A	ARG275
A	ASN303
A	HIS304
A	HIS352
A	ARG400
A	HIS427
A	VAL429
A	PHE446
A	TYR451
A	MN500
A	MN501
A	HOH852
A	HOH871
A	HOH872

---

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MN C 500

Chain	Residue
C	NHC1
C	ASP271
C	ASN303
C	HIS352
C	HIS427
C	MN501
C	HOH874

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN C 501

Chain	Residue
C	NHC1
C	ASP242
C	HIS244
C	ASP271
C	MN500

---

site_id	AC6
Number of Residues	17
Details	BINDING SITE FOR RESIDUE NHC C 1

Chain	Residue
C	ASP242
C	HIS244
C	ASP271
C	ARG275
C	ASN303
C	HIS304
C	HIS352
C	ARG400
C	HIS427
C	VAL429
C	PHE446
C	TYR451
C	MN500
C	MN501
C	HOH662
C	HOH873
C	HOH874

---

Functional Information from PROSITE/UniProt

site_id	PS00125
Number of Residues	6
Details	SER_THR_PHOSPHATASE Serine/threonine specific protein phosphatases signature. LRGNHE

Chain	Residue	Details
A	LEU300-GLU305

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:15155720

Chain	Residue	Details
A	HIS304
C	HIS304

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:15155720, ECO:0000269|PubMed:15577939, ECO:0000269|PubMed:19601647, ECO:0007744|PDB:1S95, ECO:0007744|PDB:1WAO, ECO:0007744|PDB:3H60, ECO:0007744|PDB:3H61, ECO:0007744|PDB:3H62, ECO:0007744|PDB:3H63, ECO:0007744|PDB:3H64

Chain	Residue	Details
A	ASP242
A	ASP271
A	ASN303
A	HIS352
C	ASP242
C	ASP271
C	ASN303
C	HIS352

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:15155720

Chain	Residue	Details
A	HIS244
A	ARG275
A	ARG400
A	HIS427
C	HIS244
C	ARG275
C	ARG400
C	HIS427

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1aui

Chain	Residue	Details
A	HIS304
A	ASP274

---

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1aui

Chain	Residue	Details
C	HIS304
C	ASP274

---

site_id	MCSA1
Number of Residues	10
Details	M-CSA 472

Chain	Residue	Details
A	ASP242	metal ligand
A	HIS427	activator, metal ligand
A	HIS244	metal ligand
A	ASP271	metal ligand
A	ASP274	activator, proton donor
A	ARG275	transition state stabiliser
A	ASN303	metal ligand, transition state stabiliser
A	HIS304	proton acceptor, proton donor, proton relay
A	HIS352	metal ligand
A	ARG400	transition state stabiliser

---

site_id	MCSA2
Number of Residues	10
Details	M-CSA 472

Chain	Residue	Details
C	ASP242	metal ligand
C	HIS427	activator, metal ligand
C	HIS244	metal ligand
C	ASP271	metal ligand
C	ASP274	activator, proton donor
C	ARG275	transition state stabiliser
C	ASN303	metal ligand, transition state stabiliser
C	HIS304	proton acceptor, proton donor, proton relay
C	HIS352	metal ligand
C	ARG400	transition state stabiliser

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