3HYC

Crystal structure of E. coli phosphatase YrbI, with Mg, tetragonal form

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008781	molecular_function	N-acylneuraminate cytidylyltransferase activity
A	0009103	biological_process	lipopolysaccharide biosynthetic process
A	0016787	molecular_function	hydrolase activity
A	0016788	molecular_function	hydrolase activity, acting on ester bonds
A	0019143	molecular_function	3-deoxy-manno-octulosonate-8-phosphatase activity
A	0046872	molecular_function	metal ion binding
B	0008781	molecular_function	N-acylneuraminate cytidylyltransferase activity
B	0009103	biological_process	lipopolysaccharide biosynthetic process
B	0016787	molecular_function	hydrolase activity
B	0016788	molecular_function	hydrolase activity, acting on ester bonds
B	0019143	molecular_function	3-deoxy-manno-octulosonate-8-phosphatase activity
B	0046872	molecular_function	metal ion binding
C	0008781	molecular_function	N-acylneuraminate cytidylyltransferase activity
C	0009103	biological_process	lipopolysaccharide biosynthetic process
C	0016787	molecular_function	hydrolase activity
C	0016788	molecular_function	hydrolase activity, acting on ester bonds
C	0019143	molecular_function	3-deoxy-manno-octulosonate-8-phosphatase activity
C	0046872	molecular_function	metal ion binding
D	0008781	molecular_function	N-acylneuraminate cytidylyltransferase activity
D	0009103	biological_process	lipopolysaccharide biosynthetic process
D	0016787	molecular_function	hydrolase activity
D	0016788	molecular_function	hydrolase activity, acting on ester bonds
D	0019143	molecular_function	3-deoxy-manno-octulosonate-8-phosphatase activity
D	0046872	molecular_function	metal ion binding
E	0008781	molecular_function	N-acylneuraminate cytidylyltransferase activity
E	0009103	biological_process	lipopolysaccharide biosynthetic process
E	0016787	molecular_function	hydrolase activity
E	0016788	molecular_function	hydrolase activity, acting on ester bonds
E	0019143	molecular_function	3-deoxy-manno-octulosonate-8-phosphatase activity
E	0046872	molecular_function	metal ion binding
F	0008781	molecular_function	N-acylneuraminate cytidylyltransferase activity
F	0009103	biological_process	lipopolysaccharide biosynthetic process
F	0016787	molecular_function	hydrolase activity
F	0016788	molecular_function	hydrolase activity, acting on ester bonds
F	0019143	molecular_function	3-deoxy-manno-octulosonate-8-phosphatase activity
F	0046872	molecular_function	metal ion binding
G	0008781	molecular_function	N-acylneuraminate cytidylyltransferase activity
G	0009103	biological_process	lipopolysaccharide biosynthetic process
G	0016787	molecular_function	hydrolase activity
G	0016788	molecular_function	hydrolase activity, acting on ester bonds
G	0019143	molecular_function	3-deoxy-manno-octulosonate-8-phosphatase activity
G	0046872	molecular_function	metal ion binding
H	0008781	molecular_function	N-acylneuraminate cytidylyltransferase activity
H	0009103	biological_process	lipopolysaccharide biosynthetic process
H	0016787	molecular_function	hydrolase activity
H	0016788	molecular_function	hydrolase activity, acting on ester bonds
H	0019143	molecular_function	3-deoxy-manno-octulosonate-8-phosphatase activity
H	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG A 201

Chain	Residue
A	ASP32
A	ASP34
A	ASP125

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG B 202

Chain	Residue
A	SER187
B	ASP32
B	ASP34
B	ASP125

---

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG C 203

Chain	Residue
C	ASP125
C	ASP32
C	ASP34

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG D 204

Chain	Residue
C	SER187
D	ASP32
D	ASP34
D	ASP125

---

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG E 205

Chain	Residue
E	ASP32
E	ASP34
E	ASP125

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG F 206

Chain	Residue
E	SER187
F	ASP32
F	ASP34
F	ASP125

---

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG G 207

Chain	Residue
G	ASP32
G	ASP34
G	ASP125

---

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG H 208

Chain	Residue
G	SER187
H	ASP32
H	ASP34
H	ASP125

---

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL B 204

Chain	Residue
A	SER187
B	ASP32
B	GLY77
B	LYS102

---

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL D 205

Chain	Residue
D	ASP32
D	GLY77
D	LYS102

---

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL F 189

Chain	Residue
E	SER187
F	ASP32
F	GLY77
F	LYS102
F	ILE128

---

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL G 189

Chain	Residue
G	ASP32
G	LYS102
G	ILE128

---

site_id	BC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL H 189

Chain	Residue
H	GLY77
H	LYS102

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	88
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19726684","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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