5DFA

3D structure of the E323A catalytic mutant of Gan42B, a GH42 beta-galactosidase from G. stearothermophilus

Replaces:  4OJY

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

Functional Information from PDB Data

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

Chain	Residue
A	CYS124
A	CYS164
A	CYS166
A	CYS169

---

site_id	AC2
Number of Residues	8
Details	binding site for residue GOL A 702

Chain	Residue
A	HIS625
A	HOH1019
A	HOH1059
A	GLU452
A	ARG453
A	PHE622
A	VAL623
A	LYS624

---

site_id	AC3
Number of Residues	8
Details	binding site for residue GOL A 703

Chain	Residue
A	ARG120
A	GLU159
A	ASP285
A	TYR287
A	PHE361
A	GLU371
A	HOH829
C	HOH883

---

site_id	AC4
Number of Residues	9
Details	binding site for residue GOL A 704

Chain	Residue
A	ASN330
A	HIS332
A	LYS333
A	ASN335
C	ALA429
C	GLN430
C	GLY431
C	ALA434
C	LYS437

---

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

Chain	Residue
B	CYS124
B	CYS164
B	CYS166
B	CYS169

---

site_id	AC6
Number of Residues	7
Details	binding site for residue GOL B 702

Chain	Residue
B	GLU452
B	ARG453
B	PHE622
B	VAL623
B	LYS624
B	HIS625
B	HOH820

---

site_id	AC7
Number of Residues	7
Details	binding site for residue GOL B 703

Chain	Residue
B	ARG120
B	GLU159
B	ASP285
B	TYR287
B	PHE361
B	GLU371
B	HOH963

---

site_id	AC8
Number of Residues	5
Details	binding site for residue GOL B 704

Chain	Residue
B	ARG438
B	THR442
B	ARG598
B	HOH924
B	HOH925

---

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

Chain	Residue
C	CYS124
C	CYS164
C	CYS166
C	CYS169

---

site_id	AD1
Number of Residues	6
Details	binding site for residue GOL C 702

Chain	Residue
C	GLU452
C	ARG453
C	VAL623
C	LYS624
C	HIS625
C	HOH809

---

site_id	AD2
Number of Residues	4
Details	binding site for residue GOL C 703

Chain	Residue
C	ARG438
C	THR442
C	GLN445
C	ARG598

---

site_id	AD3
Number of Residues	8
Details	binding site for residue GOL C 704

Chain	Residue
B	HOH862
C	ARG120
C	GLU159
C	ASP285
C	TYR287
C	PHE361
C	GLU371
C	HOH815

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ASP21-ILE33

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