2GK1

X-ray crystal structure of NGT-bound HexA

Functional Information from GO Data

Chain	GOid	namespace	contents
I	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
I	0004563	molecular_function	beta-N-acetylhexosaminidase activity
I	0005975	biological_process	carbohydrate metabolic process
J	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
J	0004563	molecular_function	beta-N-acetylhexosaminidase activity
J	0005975	biological_process	carbohydrate metabolic process
K	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
K	0004563	molecular_function	beta-N-acetylhexosaminidase activity
K	0005975	biological_process	carbohydrate metabolic process
L	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
L	0004563	molecular_function	beta-N-acetylhexosaminidase activity
L	0005975	biological_process	carbohydrate metabolic process
M	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
M	0004563	molecular_function	beta-N-acetylhexosaminidase activity
M	0005975	biological_process	carbohydrate metabolic process
N	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
N	0004563	molecular_function	beta-N-acetylhexosaminidase activity
N	0005975	biological_process	carbohydrate metabolic process
O	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
O	0004563	molecular_function	beta-N-acetylhexosaminidase activity
O	0005975	biological_process	carbohydrate metabolic process
P	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
P	0004563	molecular_function	beta-N-acetylhexosaminidase activity
P	0005975	biological_process	carbohydrate metabolic process
Q	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
Q	0004563	molecular_function	beta-N-acetylhexosaminidase activity
Q	0005975	biological_process	carbohydrate metabolic process
R	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
R	0004563	molecular_function	beta-N-acetylhexosaminidase activity
R	0005975	biological_process	carbohydrate metabolic process
S	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
S	0004563	molecular_function	beta-N-acetylhexosaminidase activity
S	0005975	biological_process	carbohydrate metabolic process
T	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
T	0004563	molecular_function	beta-N-acetylhexosaminidase activity
T	0005975	biological_process	carbohydrate metabolic process

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Region: {"description":"Critical for hydrolysis GM2 gangliosides"}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"16698036","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"1533633","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16698036","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11707436","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"1533633","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16698036","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11707436","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"11447134","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	8
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"11447134","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"11329289","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	4
Details	Site: {"description":"Not glycosylated","evidences":[{"source":"PubMed","id":"11447134","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"11447134","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12754519","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1qba

Chain	Residue	Details
B	ASP354
B	GLU355

---

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1qba

Chain	Residue	Details
D	ASP354
D	GLU355

---

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1qba

Chain	Residue	Details
F	ASP354
F	GLU355

---

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1qba

Chain	Residue	Details
H	ASP354
H	GLU355

---

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1qba

Chain	Residue	Details
A	GLU323
A	ASP322

---

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1qba

Chain	Residue	Details
C	GLU323
C	ASP322

---

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 1qba

Chain	Residue	Details
E	GLU323
E	ASP322

---

site_id	CSA8
Number of Residues	2
Details	Annotated By Reference To The Literature 1qba

Chain	Residue	Details
G	GLU323
G	ASP322

---