3N28

Crystal structure of probable phosphoserine phosphatase from vibrio cholerae, unliganded form

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0005737	cellular_component	cytoplasm
A	0006564	biological_process	L-serine biosynthetic process
A	0016787	molecular_function	hydrolase activity
A	0036424	molecular_function	L-phosphoserine phosphatase activity
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 A 336

Chain	Residue
A	THR81
A	SER82

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 337

Chain	Residue
A	THR117
A	GLY270
A	ALA271
A	ASN272
A	LYS289

---

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 A 338

Chain	Residue
A	ARG20
A	TYR43

---

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 A 339

Chain	Residue
A	PRO22
A	GLU23

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 340

Chain	Residue
A	ALA31
A	LYS32
A	LYS33
A	GLN320

---

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 341

Chain	Residue
A	VAL228
A	SER229
A	GLY230

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Nucleophile => ECO:0000250|UniProtKB:Q58989

Chain	Residue	Details
A	ASP113

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q58989

Chain	Residue	Details
A	ASP115

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000250|UniProtKB:Q58989

Chain	Residue	Details
A	ASP113
A	GLU122
A	ARG158
A	SER201
A	LYS246
A	ASP269
A	ASN272
A	ASP115

---