4MOY

Structure of a second nuclear PP1 Holoenzyme, crystal form 1

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016787	molecular_function	hydrolase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MN A 401

Chain	Residue
A	ASP64
A	HIS66
A	ASP92
A	MN402
A	PO4404
A	HOH633
A	HOH634

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site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MN A 402

Chain	Residue
A	HIS173
A	HIS248
A	MN401
A	PO4404
A	HOH634
A	ASP92
A	ASN124

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL A 403

Chain	Residue
A	GLY215
A	GLY228
A	ALA229
A	GLU230
A	VAL231

---

site_id	AC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PO4 A 404

Chain	Residue
A	HIS66
A	ASP92
A	ARG96
A	ASN124
A	HIS125
A	ARG221
A	HIS248
A	MN401
A	MN402
A	HOH633
A	HOH634

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 405

Chain	Residue
A	PRO50
A	GLU54
A	GLU116
A	PHE119

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 406

Chain	Residue
A	CYS127
A	SER129
A	VAL195
A	HOH538

---

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	LEU121-GLU126

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by PKA => ECO:0000269|PubMed:12574161

Chain	Residue	Details
B	THR398

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:30100357, ECO:0000269|PubMed:35830882, ECO:0000269|PubMed:35831509, ECO:0000269|PubMed:36175670, ECO:0007744|PDB:6CZO, ECO:0007744|PDB:7TVF, ECO:0007744|PDB:7TXH, ECO:0007744|PDB:7UPI

Chain	Residue	Details
A	ASP64
A	HIS66
A	ASP92
A	ASN124
A	HIS173
A	HIS248

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER22

---