Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3LK6

Beta-N-hexosaminidase N318D mutant (YBBD_N318D) from bacillus subtilis

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
A	0004563	molecular_function	beta-N-acetylhexosaminidase activity
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0005975	biological_process	carbohydrate metabolic process
A	0008360	biological_process	regulation of cell shape
A	0009252	biological_process	peptidoglycan biosynthetic process
A	0009254	biological_process	peptidoglycan turnover
A	0016231	molecular_function	beta-N-acetylglucosaminidase activity
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0071555	biological_process	cell wall organization
B	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
B	0004563	molecular_function	beta-N-acetylhexosaminidase activity
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0005975	biological_process	carbohydrate metabolic process
B	0008360	biological_process	regulation of cell shape
B	0009252	biological_process	peptidoglycan biosynthetic process
B	0009254	biological_process	peptidoglycan turnover
B	0016231	molecular_function	beta-N-acetylglucosaminidase activity
B	0016787	molecular_function	hydrolase activity
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0071555	biological_process	cell wall organization
C	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
C	0004563	molecular_function	beta-N-acetylhexosaminidase activity
C	0005829	cellular_component	cytosol
C	0005886	cellular_component	plasma membrane
C	0005975	biological_process	carbohydrate metabolic process
C	0008360	biological_process	regulation of cell shape
C	0009252	biological_process	peptidoglycan biosynthetic process
C	0009254	biological_process	peptidoglycan turnover
C	0016231	molecular_function	beta-N-acetylglucosaminidase activity
C	0016787	molecular_function	hydrolase activity
C	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
C	0071555	biological_process	cell wall organization
D	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
D	0004563	molecular_function	beta-N-acetylhexosaminidase activity
D	0005829	cellular_component	cytosol
D	0005886	cellular_component	plasma membrane
D	0005975	biological_process	carbohydrate metabolic process
D	0008360	biological_process	regulation of cell shape
D	0009252	biological_process	peptidoglycan biosynthetic process
D	0009254	biological_process	peptidoglycan turnover
D	0016231	molecular_function	beta-N-acetylglucosaminidase activity
D	0016787	molecular_function	hydrolase activity
D	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
D	0071555	biological_process	cell wall organization

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PEG A 643

Chain	Residue
A	LYS479
A	ILE481
A	LYS482

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG A 644

Chain	Residue
A	ASN152
A	GLN155
A	LYS429
A	LYS433

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PEG A 645

Chain	Residue
A	HIS222
A	ASN318

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG A 646

Chain	Residue
A	ARG148
A	SER149
A	ARG150
A	ILE151

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA A 647

Chain	Residue
A	THR106
A	ASP107
A	LEU167
A	GLY168
A	LYS410

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PEG B 643

Chain	Residue
B	LYS479
B	ILE481
B	LYS482

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PEG B 644

Chain	Residue
B	ARG148
B	SER149
B	ARG150
B	ILE151
B	ARG202

site_id	AC8
Number of Residues	1
Details	BINDING SITE FOR RESIDUE PEG B 645

Chain	Residue
B	ILE151

site_id	AC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PEG B 648

Chain	Residue
B	HIS222
B	ASN318

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PEG B 649

Chain	Residue
B	ASN182
B	ASP184
B	ASP230

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG B 650

Chain	Residue
B	ASN152
B	GLN155
B	LYS429
B	LYS433

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA B 651

Chain	Residue
B	THR106
B	ASP107
B	LEU167
B	GLY168
B	LYS410

site_id	BC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE PEG C 647

Chain	Residue
C	THR280

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PEG C 643

Chain	Residue
C	LYS479
C	ILE481
C	LYS482

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PEG C 644

Chain	Residue
C	ARG148
C	SER149
C	ARG150
C	ILE151
C	ARG202

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PEG C 645

Chain	Residue
C	ASN152
C	GLN155
C	ALA426
C	LYS429
C	LYS433

site_id	BC8
Number of Residues	1
Details	BINDING SITE FOR RESIDUE PEG C 646

Chain	Residue
C	HIS222

site_id	BC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA C 648

Chain	Residue
C	THR106
C	ASP107
C	GLY168
C	LYS410

site_id	CC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PEG D 643

Chain	Residue
D	HIS222
D	HIS226

site_id	CC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG D 644

Chain	Residue
D	ASN152
D	GLN155
D	LYS429
D	LYS433

site_id	CC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PEG D 645

Chain	Residue
D	ARG148
D	SER149
D	ARG150
D	ILE151
D	ARG202

site_id	CC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PEG D 646

Chain	Residue
D	LYS479
D	LYS482

site_id	CC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA D 647

Chain	Residue
D	THR106
D	ASP107
D	LEU167
D	GLY168
D	LYS410

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"20826810","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"23177201","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"20826810","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"23177201","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20826810","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23177201","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Site: {"description":"Important for catalytic activity","evidences":[{"source":"PubMed","id":"20826810","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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