5E9A

Crystal structure analysis of the cold-adamped beta-galactosidase from Rahnella sp. R3

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004565	molecular_function	beta-galactosidase activity
A	0005975	biological_process	carbohydrate metabolic process
A	0006012	biological_process	galactose metabolic process
A	0009341	cellular_component	beta-galactosidase complex
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0046872	molecular_function	metal ion binding
B	0004565	molecular_function	beta-galactosidase activity
B	0005975	biological_process	carbohydrate metabolic process
B	0006012	biological_process	galactose metabolic process
B	0009341	cellular_component	beta-galactosidase complex
B	0016787	molecular_function	hydrolase activity
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0046872	molecular_function	metal ion binding
C	0004565	molecular_function	beta-galactosidase activity
C	0005975	biological_process	carbohydrate metabolic process
C	0006012	biological_process	galactose metabolic process
C	0009341	cellular_component	beta-galactosidase complex
C	0016787	molecular_function	hydrolase activity
C	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
C	0046872	molecular_function	metal ion binding
D	0004565	molecular_function	beta-galactosidase activity
D	0005975	biological_process	carbohydrate metabolic process
D	0006012	biological_process	galactose metabolic process
D	0009341	cellular_component	beta-galactosidase complex
D	0016787	molecular_function	hydrolase activity
D	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
D	0046872	molecular_function	metal ion binding
E	0004565	molecular_function	beta-galactosidase activity
E	0005975	biological_process	carbohydrate metabolic process
E	0006012	biological_process	galactose metabolic process
E	0009341	cellular_component	beta-galactosidase complex
E	0016787	molecular_function	hydrolase activity
E	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
E	0046872	molecular_function	metal ion binding
F	0004565	molecular_function	beta-galactosidase activity
F	0005975	biological_process	carbohydrate metabolic process
F	0006012	biological_process	galactose metabolic process
F	0009341	cellular_component	beta-galactosidase complex
F	0016787	molecular_function	hydrolase activity
F	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
F	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue ZN A 701

Chain	Residue
A	CYS122
A	CYS162
A	CYS164
A	CYS167

---

site_id	AC2
Number of Residues	5
Details	binding site for residue ACT A 702

Chain	Residue
A	ARG118
A	ASN156
A	GLU157
A	GLU314
A	GLU362

---

site_id	AC3
Number of Residues	4
Details	binding site for residue ZN B 701

Chain	Residue
B	CYS122
B	CYS162
B	CYS164
B	CYS167

---

site_id	AC4
Number of Residues	4
Details	binding site for residue ACT B 702

Chain	Residue
B	ARG118
B	GLU157
B	GLU314
B	GLU362

---

site_id	AC5
Number of Residues	4
Details	binding site for residue ZN C 701

Chain	Residue
C	CYS122
C	CYS162
C	CYS164
C	CYS167

---

site_id	AC6
Number of Residues	3
Details	binding site for residue ACT C 702

Chain	Residue
C	ARG118
C	GLU314
C	GLU362

---

site_id	AC7
Number of Residues	4
Details	binding site for residue ZN D 701

Chain	Residue
D	CYS122
D	CYS162
D	CYS164
D	CYS167

---

site_id	AC8
Number of Residues	5
Details	binding site for residue ACT D 702

Chain	Residue
D	ARG118
D	ASN156
D	GLU157
D	GLU314
D	GLU362

---

site_id	AC9
Number of Residues	4
Details	binding site for residue ZN E 701

Chain	Residue
E	CYS122
E	CYS162
E	CYS164
E	CYS167

---

site_id	AD1
Number of Residues	5
Details	binding site for residue ACT E 702

Chain	Residue
E	ARG118
E	GLU314
E	GLU362
E	HOH818
E	HOH825

---

site_id	AD2
Number of Residues	4
Details	binding site for residue ZN F 701

Chain	Residue
F	CYS122
F	CYS162
F	CYS164
F	CYS167

---

site_id	AD3
Number of Residues	5
Details	binding site for residue ACT F 702

Chain	Residue
F	ARG118
F	GLU157
F	GLU314
F	GLU362
F	HOH842

---

Functional Information from PROSITE/UniProt

site_id	PS00018
Number of Residues	13
Details	EF_HAND_1 EF-hand calcium-binding domain. DYNPEQWLDhpDV

Chain	Residue	Details
A	ASP19-VAL31

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