Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2XN1

Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM with TRIS

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
A	0004557	molecular_function	alpha-galactosidase activity
A	0005975	biological_process	carbohydrate metabolic process
A	0016052	biological_process	carbohydrate catabolic process
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0051289	biological_process	protein homotetramerization
A	1901545	biological_process	response to raffinose
B	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
B	0004557	molecular_function	alpha-galactosidase activity
B	0005975	biological_process	carbohydrate metabolic process
B	0016052	biological_process	carbohydrate catabolic process
B	0016787	molecular_function	hydrolase activity
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0051289	biological_process	protein homotetramerization
B	1901545	biological_process	response to raffinose
C	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
C	0004557	molecular_function	alpha-galactosidase activity
C	0005975	biological_process	carbohydrate metabolic process
C	0016052	biological_process	carbohydrate catabolic process
C	0016787	molecular_function	hydrolase activity
C	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
C	0051289	biological_process	protein homotetramerization
C	1901545	biological_process	response to raffinose
D	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
D	0004557	molecular_function	alpha-galactosidase activity
D	0005975	biological_process	carbohydrate metabolic process
D	0016052	biological_process	carbohydrate catabolic process
D	0016787	molecular_function	hydrolase activity
D	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
D	0051289	biological_process	protein homotetramerization
D	1901545	biological_process	response to raffinose

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE TRS A 1733

Chain	Residue
A	TRP340
A	ASP552
A	GOL1734
A	HOH2242
A	ASP370
A	TRP415
A	LYS480
A	ASP482
A	ASN484
A	CYS530
A	GLY532
A	GLY533

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 1734

Chain	Residue
A	ASN484
A	GLY532
A	TRS1733
A	HOH2453
B	GLY58
B	PHE59

site_id	AC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE TRS B 1733

Chain	Residue
B	TRP340
B	ASP370
B	TRP415
B	LYS480
B	ASP482
B	ASN484
B	CYS530
B	GLY532
B	GLY533
B	ASP552
B	GOL1734

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL B 1734

Chain	Residue
A	PHE59
B	ARG447
B	ASN484
B	GLY532
B	TRS1733
B	HOH2438

site_id	AC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE TRS C 1733

Chain	Residue
C	TRP340
C	ASP370
C	TRP415
C	LYS480
C	ASP482
C	ASN484
C	CYS530
C	GLY532
C	GLY533
C	ASP552
C	GOL1734

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL C 1734

Chain	Residue
C	ASN484
C	GLY532
C	TRS1733
C	HOH2483
C	HOH2484
D	PHE59

site_id	AC7
Number of Residues	11
Details	BINDING SITE FOR RESIDUE TRS D 1733

Chain	Residue
D	TRP340
D	ASP370
D	TRP415
D	LYS480
D	ASP482
D	ASN484
D	CYS530
D	GLY532
D	GLY533
D	ASP552
D	GOL1734

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL D 1734

Chain	Residue
C	GLY58
C	PHE59
D	ASN484
D	GLY532
D	TRS1733
D	HOH2389

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 1735

Chain	Residue
A	LYS147
A	GLY173
A	GLU174
A	GLU175
A	HOH2097

site_id	BC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE GOL D 1735

Chain	Residue
C	TYR224
C	TYR282
C	SER488
C	HOH2326
D	ALA83
D	GLY84
D	GLU85
D	MET86
D	ASP87
D	PHE88
D	HOH2049

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL B 1735

Chain	Residue
B	ASN695
B	PHE702
B	PHE712
B	TYR726
B	PHE728
C	HOH2030

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL B 1736

Chain	Residue
B	LYS147
B	GLY173
B	GLU174
B	GLU175
B	HOH2098
B	HOH2439

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL C 1735

Chain	Residue
C	GLU174
C	GLU175
C	HOH2098
C	VAL145
C	GLY173

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL D 1736

Chain	Residue
D	GLY173
D	GLU174
D	GLU175
D	HOH2082
D	HOH2390

site_id	BC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL A 1736

Chain	Residue
A	GLY32
A	THR33
A	LEU34
A	ARG73
A	LYS78
A	TYR80
A	GLU85
A	LEU106
A	ALA107

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL B 1737

Chain	Residue
B	ILE332
B	PRO334
B	GLU365
B	LYS411
B	HOH2236

site_id	BC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL C 1736

Chain	Residue
C	LYS457
C	ARG460
C	ASP461
C	PHE464
C	ASP513
C	LEU514
C	LYS517

site_id	BC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL B 1738

Chain	Residue
B	HIS674
B	ALA675
B	ILE716
B	GLU717
B	ARG718
C	LEU55

site_id	CC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 1737

Chain	Residue
A	ASN695
A	PHE702
A	PHE712
A	PHE728
A	HOH2454
A	HOH2455
D	GLN49
D	HOH2023

site_id	CC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL A 1738

Chain	Residue
A	ALA83
A	GLY84
A	GLU85
A	MET86
A	ASP87
A	PHE88
A	HOH2067
B	TYR224
B	TYR282
B	SER488

site_id	CC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE GOL B 1739

Chain	Residue
A	TYR224
A	TYR282
A	SER488
A	HOH2299
B	ALA83
B	GLY84
B	GLU85
B	MET86
B	ASP87
B	PHE88
B	HOH2073

site_id	CC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL C 1737

Chain	Residue
C	ALA83
C	GLY84
C	GLU85
C	MET86
C	ASP87
C	PHE88
C	HOH2070
D	TYR224
D	TYR282
D	SER488

site_id	CC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL B 1740

Chain	Residue
B	GLY32
B	THR33
B	LEU34
B	ARG73
B	LYS78
B	TYR80
B	GLU85
B	LEU106
B	LEU141

site_id	CC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL D 1737

Chain	Residue
D	GLY32
D	THR33
D	LEU34
D	ARG73
D	LYS78
D	TYR80
D	SER81
D	GLU85
D	LEU106
D	LEU141

site_id	CC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL C 1738

Chain	Residue
C	GLY32
C	THR33
C	LEU34
C	LYS78
C	TYR80
C	GLU85
C	LEU106
C	ALA107
C	LEU141

Functional Information from PROSITE/UniProt

site_id	PS00512
Number of Residues	16
Details	ALPHA_GALACTOSIDASE Alpha-galactosidase signature. GLemFvLDDg.Wfgh....RD

Chain	Residue	Details
A	GLY363-ASP378

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"21827767","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"21827767","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	44
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21827767","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2XN2","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)