3ESR

Crystal Structure of D,D-heptose1.7-bisphosphate phosphatase from E. coli in complex with calcium and phosphate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005975	biological_process	carbohydrate metabolic process
A	0008270	molecular_function	zinc ion binding
A	0009103	biological_process	lipopolysaccharide biosynthetic process
A	0009244	biological_process	lipopolysaccharide core region biosynthetic process
A	0016787	molecular_function	hydrolase activity
A	0016791	molecular_function	phosphatase activity
A	0034200	molecular_function	D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase activity
A	0046872	molecular_function	metal ion binding
A	0097171	biological_process	ADP-L-glycero-beta-D-manno-heptose biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 212

Chain	Residue
A	CYS112
A	HIS114
A	CYS127
A	CYS129

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 213

Chain	Residue
A	ASP31
A	ASP33
A	ASP156
A	PO4214
A	HOH304

---

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PO4 A 214

Chain	Residue
A	ASP31
A	ARG32
A	ASP33
A	THR73
A	ASN74
A	LYS131
A	CA213
A	HOH243
A	HOH316

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Nucleophile => ECO:0000269|PubMed:20050699

Chain	Residue	Details
A	ASP31

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000269|PubMed:20050614, ECO:0000269|PubMed:20050699

Chain	Residue	Details
A	ASP33

---

site_id	SWS_FT_FI3
Number of Residues	10
Details	BINDING: BINDING => ECO:0000269|PubMed:20050614

Chain	Residue	Details
A	ASP31
A	LYS157
A	ASP33
A	ASP39
A	CYS112
A	HIS114
A	CYS127
A	CYS129
A	ARG130
A	ASP156

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:20050614, ECO:0000269|PubMed:20050699

Chain	Residue	Details
A	THR73

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	SITE: Stabilizes the phosphoryl group => ECO:0000269|PubMed:20050614, ECO:0000269|PubMed:20050699

Chain	Residue	Details
A	THR73

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	SITE: Contributes to substrate recognition => ECO:0000269|PubMed:20050614

Chain	Residue	Details
A	ARG130

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	SITE: Stabilizes the phosphoryl group => ECO:0000269|PubMed:20050614

Chain	Residue	Details
A	LYS131

---

Catalytic Information from CSA

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

Chain	Residue	Details
A	ALA100
A	LYS131

---

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

Chain	Residue	Details
A	LYS131
A	THR73

---