3L8E

Crystal Structure of apo form of D,D-heptose 1.7-bisphosphate phosphatase from E. Coli

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN A 801

Chain	Residue
A	CYS92
A	HIS94
A	CYS107
A	CYS109
A	ARG110

---

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE ACY A 901

Chain	Residue
A	ASN54
A	LYS111
A	LYS137
A	HOH202
A	ASP11
A	ARG12
A	ASP13
A	THR53

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN B 802

Chain	Residue
B	CYS92
B	HIS94
B	CYS107
B	CYS109
B	ARG110

---

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE ACY B 902

Chain	Residue
B	ASP11
B	ARG12
B	ASP13
B	THR53
B	ASN54
B	LYS111
B	LYS137
B	HOH193

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Nucleophile => ECO:0000269|PubMed:20050699

Chain	Residue	Details
A	ASP11
B	ASP11

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Proton donor => ECO:0000269|PubMed:20050614, ECO:0000269|PubMed:20050699

Chain	Residue	Details
A	ASP13
B	ASP13

---

site_id	SWS_FT_FI3
Number of Residues	20
Details	BINDING: BINDING => ECO:0000269|PubMed:20050614

Chain	Residue	Details
A	ASP11
A	CYS109
A	ARG110
A	ASP136
A	LYS137
B	ASP11
B	ASP13
B	ASP19
B	CYS92
B	HIS94
B	CYS107
B	CYS109
B	ARG110
B	ASP136
B	LYS137
A	ASP13
A	ASP19
A	CYS92
A	HIS94
A	CYS107

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:20050614, ECO:0000269|PubMed:20050699

Chain	Residue	Details
A	THR53
B	THR53

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	SITE: Stabilizes the phosphoryl group => ECO:0000269|PubMed:20050614, ECO:0000269|PubMed:20050699

Chain	Residue	Details
A	THR53
B	THR53

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	SITE: Contributes to substrate recognition => ECO:0000269|PubMed:20050614

Chain	Residue	Details
A	ARG110
B	ARG110

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	SITE: Stabilizes the phosphoryl group => ECO:0000269|PubMed:20050614

Chain	Residue	Details
A	LYS111
B	LYS111

---