1NMM
beta-1,4-galactosyltransferase mutant Cys342Thr complex with alpha-lactalbumin and GlcNAc
Replaces: 1JN8Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004461 | molecular_function | lactose synthase activity |
A | 0005509 | molecular_function | calcium ion binding |
A | 0005515 | molecular_function | protein binding |
A | 0005576 | cellular_component | extracellular region |
A | 0005989 | biological_process | lactose biosynthetic process |
A | 0032991 | cellular_component | protein-containing complex |
A | 0046872 | molecular_function | metal ion binding |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0016757 | molecular_function | glycosyltransferase activity |
C | 0004461 | molecular_function | lactose synthase activity |
C | 0005509 | molecular_function | calcium ion binding |
C | 0005515 | molecular_function | protein binding |
C | 0005576 | cellular_component | extracellular region |
C | 0005989 | biological_process | lactose biosynthetic process |
C | 0032991 | cellular_component | protein-containing complex |
C | 0046872 | molecular_function | metal ion binding |
D | 0005975 | biological_process | carbohydrate metabolic process |
D | 0016757 | molecular_function | glycosyltransferase activity |
Functional Information from PROSITE/UniProt
site_id | PS00128 |
Number of Residues | 19 |
Details | GLYCOSYL_HYDROL_F22_1 Glycosyl hydrolases family 22 (GH22) domain signature. CgisCdkLlddELdddiaC |
Chain | Residue | Details |
A | CYS73-CYS91 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 16 |
Details | BINDING: |
Chain | Residue | Details |
B | PRO187 | |
D | PHE226 | |
D | VAL253 | |
D | ASP254 | |
D | TRP314 | |
D | GLY316 | |
D | HIS347 | |
D | ARG359 | |
B | PHE226 | |
B | VAL253 | |
B | ASP254 | |
B | TRP314 | |
B | GLY316 | |
B | HIS347 | |
B | ARG359 | |
D | PRO187 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN45 | |
C | ASN45 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1fr8 |
Chain | Residue | Details |
B | ARG359 | |
B | GLU317 | |
B | ASP319 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1fr8 |
Chain | Residue | Details |
D | ARG359 | |
D | GLU317 | |
D | ASP319 |
site_id | MCSA1 |
Number of Residues | 8 |
Details | M-CSA 570 |
Chain | Residue | Details |
B | ASP252 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
B | ASP254 | metal ligand |
B | TRP314 | electrostatic stabiliser, hydrogen bond donor |
B | GLU317 | electrostatic stabiliser, hydrogen bond acceptor |
B | ASP318 | activator, electrostatic stabiliser, proton acceptor, proton donor |
B | MET344 | metal ligand |
B | HIS347 | metal ligand |
B | ARG349 | electrostatic stabiliser, hydrogen bond donor |
site_id | MCSA2 |
Number of Residues | 8 |
Details | M-CSA 570 |
Chain | Residue | Details |
D | ASP252 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
D | ASP254 | metal ligand |
D | TRP314 | electrostatic stabiliser, hydrogen bond donor |
D | GLU317 | electrostatic stabiliser, hydrogen bond acceptor |
D | ASP318 | activator, electrostatic stabiliser, proton acceptor, proton donor |
D | MET344 | metal ligand |
D | HIS347 | metal ligand |
D | ARG349 | electrostatic stabiliser, hydrogen bond donor |