Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1XSJ

Structure of a Family 31 alpha glycosidase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
A	0005975	biological_process	carbohydrate metabolic process
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0030246	molecular_function	carbohydrate binding
A	0042802	molecular_function	identical protein binding
A	0061634	molecular_function	alpha-D-xyloside xylohydrolase activity
A	0080176	molecular_function	xyloglucan 1,6-alpha-xylosidase activity
B	0003824	molecular_function	catalytic activity
B	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
B	0005975	biological_process	carbohydrate metabolic process
B	0016787	molecular_function	hydrolase activity
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0030246	molecular_function	carbohydrate binding
B	0042802	molecular_function	identical protein binding
B	0061634	molecular_function	alpha-D-xyloside xylohydrolase activity
B	0080176	molecular_function	xyloglucan 1,6-alpha-xylosidase activity
C	0003824	molecular_function	catalytic activity
C	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
C	0005975	biological_process	carbohydrate metabolic process
C	0016787	molecular_function	hydrolase activity
C	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
C	0030246	molecular_function	carbohydrate binding
C	0042802	molecular_function	identical protein binding
C	0061634	molecular_function	alpha-D-xyloside xylohydrolase activity
C	0080176	molecular_function	xyloglucan 1,6-alpha-xylosidase activity
D	0003824	molecular_function	catalytic activity
D	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
D	0005975	biological_process	carbohydrate metabolic process
D	0016787	molecular_function	hydrolase activity
D	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
D	0030246	molecular_function	carbohydrate binding
D	0042802	molecular_function	identical protein binding
D	0061634	molecular_function	alpha-D-xyloside xylohydrolase activity
D	0080176	molecular_function	xyloglucan 1,6-alpha-xylosidase activity
E	0003824	molecular_function	catalytic activity
E	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
E	0005975	biological_process	carbohydrate metabolic process
E	0016787	molecular_function	hydrolase activity
E	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
E	0030246	molecular_function	carbohydrate binding
E	0042802	molecular_function	identical protein binding
E	0061634	molecular_function	alpha-D-xyloside xylohydrolase activity
E	0080176	molecular_function	xyloglucan 1,6-alpha-xylosidase activity
F	0003824	molecular_function	catalytic activity
F	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
F	0005975	biological_process	carbohydrate metabolic process
F	0016787	molecular_function	hydrolase activity
F	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
F	0030246	molecular_function	carbohydrate binding
F	0042802	molecular_function	identical protein binding
F	0061634	molecular_function	alpha-D-xyloside xylohydrolase activity
F	0080176	molecular_function	xyloglucan 1,6-alpha-xylosidase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE TRS A 2001

Chain	Residue
A	PHE277
A	HIS540
A	TRS2002
A	ASP306
A	LYS414
A	ASP416
A	PHE417
A	ARG466
A	TRP479
A	ASP482
A	PHE515

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE TRS A 2002

Chain	Residue
A	ASP185
A	PHE417
A	ARG466
A	ASP482
A	TRS2001
B	ASP49
D	TRP8

site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE TRS B 2003

Chain	Residue
B	ASP306
B	LYS414
B	ASP416
B	PHE417
B	ARG466
B	TRP479
B	ASP482
B	PHE515
B	HIS540
B	TRS2004

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE TRS B 2004

Chain	Residue
B	ASP185
B	TRP380
B	PHE417
B	ARG466
B	ASP482
B	TRS2003
B	HOH2152
C	TRP8
F	ASP49

site_id	AC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE TRS C 2005

Chain	Residue
C	ASP306
C	LYS414
C	ASP416
C	PHE417
C	ARG466
C	TRP479
C	ASP482
C	PHE515
C	HIS540
C	TRS2006

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE TRS C 2006

Chain	Residue
B	TRP8
C	ASP185
C	PHE417
C	ARG466
C	ASP482
C	TRS2005
C	HOH2232
D	ASP49

site_id	AC7
Number of Residues	10
Details	BINDING SITE FOR RESIDUE TRS D 2007

Chain	Residue
A	TRS2008
D	ASP306
D	LYS414
D	ASP416
D	PHE417
D	ARG466
D	TRP479
D	ASP482
D	PHE515
D	HIS540

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE TRS A 2008

Chain	Residue
A	TRP8
D	ASP185
D	TRP380
D	ARG466
D	ASP482
D	TRS2007
E	ASP49

site_id	AC9
Number of Residues	10
Details	BINDING SITE FOR RESIDUE TRS E 2009

Chain	Residue
E	ASP306
E	LYS414
E	ASP416
E	PHE417
E	ARG466
E	TRP479
E	ASP482
E	PHE515
E	HIS540
E	TRS2010

site_id	BC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE TRS E 2010

Chain	Residue
C	ASP49
E	ASP185
E	PHE417
E	ARG466
E	ASP482
E	TRS2009
E	HOH2044
F	TRP8

site_id	BC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE TRS F 2011

Chain	Residue
F	HIS540
E	TRS2012
F	ASP306
F	LYS414
F	ASP416
F	PHE417
F	ARG466
F	TRP479
F	ASP482
F	PHE515

site_id	BC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE TRS E 2012

Chain	Residue
A	ASP49
E	TRP8
F	ASP185
F	PHE417
F	ARG466
F	ASP482
F	TRS2011
F	HOH2129

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"15501829","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	6
Details	Active site: {"evidences":[{"source":"PubMed","id":"15501829","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	6
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"15501829","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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