6HYJ

PSPH Human phosphoserine phosphatase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0001701	biological_process	in utero embryonic development
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006563	biological_process	L-serine metabolic process
A	0006564	biological_process	L-serine biosynthetic process
A	0009612	biological_process	response to mechanical stimulus
A	0016787	molecular_function	hydrolase activity
A	0031667	biological_process	response to nutrient levels
A	0033574	biological_process	response to testosterone
A	0036424	molecular_function	L-phosphoserine phosphatase activity
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
A	0046872	molecular_function	metal ion binding
B	0000287	molecular_function	magnesium ion binding
B	0001701	biological_process	in utero embryonic development
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006563	biological_process	L-serine metabolic process
B	0006564	biological_process	L-serine biosynthetic process
B	0009612	biological_process	response to mechanical stimulus
B	0016787	molecular_function	hydrolase activity
B	0031667	biological_process	response to nutrient levels
B	0033574	biological_process	response to testosterone
B	0036424	molecular_function	L-phosphoserine phosphatase activity
B	0042802	molecular_function	identical protein binding
B	0042803	molecular_function	protein homodimerization activity
B	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	binding site for residue SEP A 301

Chain	Residue
A	ASP20
A	HOH408
A	HOH413
A	HOH416
A	HOH422
A	HOH439
A	MET52
A	GLY53
A	SER109
A	GLY110
A	LYS158
A	THR182
A	HOH401
A	HOH403

---

site_id	AC2
Number of Residues	6
Details	binding site for residue CA A 302

Chain	Residue
A	ASP20
A	ASP22
A	ASP179
A	HOH416
A	HOH422
A	HOH424

---

site_id	AC3
Number of Residues	4
Details	binding site for residue SEP B 301

Chain	Residue
B	PHE131
B	PRO151
B	LYS168
B	HOH401

---

site_id	AC4
Number of Residues	6
Details	binding site for residue CA B 302

Chain	Residue
B	ASP20
B	ASP22
B	ASP179
B	HOH420
B	HOH459
B	HOH467

---

site_id	AC5
Number of Residues	5
Details	binding site for residue SER B 303

Chain	Residue
A	GLN203
A	LYS206
A	ASP207
B	GLU29
B	ARG202

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Nucleophile => ECO:0000305|PubMed:31205021, ECO:0007744|PDB:6HYJ, ECO:0007744|PDB:6HYY, ECO:0007744|PDB:6Q6J

Chain	Residue	Details
A	ASP20
B	ASP20

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Proton donor => ECO:0000305|PubMed:31205021, ECO:0007744|PDB:6HYJ, ECO:0007744|PDB:6HYY, ECO:0007744|PDB:6Q6J

Chain	Residue	Details
A	ASP22
B	ASP22

---

site_id	SWS_FT_FI3
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:31205021, ECO:0007744|PDB:6HYY

Chain	Residue	Details
A	ASP20
A	ASP22
A	ASP179
B	ASP20
B	ASP22
B	ASP179

---

site_id	SWS_FT_FI4
Number of Residues	10
Details	BINDING: BINDING => ECO:0000269|PubMed:31205021, ECO:0007744|PDB:6HYJ, ECO:0007744|PDB:6HYY, ECO:0007744|PDB:6Q6J

Chain	Residue	Details
A	MET52
B	THR182
A	GLY53
A	SER109
A	LYS158
A	THR182
B	MET52
B	GLY53
B	SER109
B	LYS158

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: N-acetylmethionine => ECO:0007744|PubMed:19413330

Chain	Residue	Details
A	MET1
B	MET1

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