2VXM
Screening a Limited Structure-based Library Identifies UDP-GalNAc- Specific Mutants of alpha-1,3 Galactosyltransferase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0016020 | cellular_component | membrane |
A | 0016758 | molecular_function | hexosyltransferase activity |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0016020 | cellular_component | membrane |
B | 0016758 | molecular_function | hexosyltransferase activity |
C | 0005975 | biological_process | carbohydrate metabolic process |
C | 0016020 | cellular_component | membrane |
C | 0016758 | molecular_function | hexosyltransferase activity |
D | 0005975 | biological_process | carbohydrate metabolic process |
D | 0016020 | cellular_component | membrane |
D | 0016758 | molecular_function | hexosyltransferase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL B 1340 |
Chain | Residue |
B | MET100 |
B | HOH2026 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MPD B 1339 |
Chain | Residue |
B | GLU96 |
B | TYR251 |
B | HOH2025 |
C | ARG138 |
C | HIS142 |
C | TYR143 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:11179209, ECO:0007744|PDB:1G8O |
Chain | Residue | Details |
A | GLU317 | |
B | GLU317 | |
C | GLU317 | |
D | GLU317 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11179209, ECO:0000269|PubMed:11592969, ECO:0000269|PubMed:12011052, ECO:0007744|PDB:1G93, ECO:0007744|PDB:1GWV, ECO:0007744|PDB:1GWW, ECO:0007744|PDB:1GX0, ECO:0007744|PDB:1GX4, ECO:0007744|PDB:1K4V, ECO:0007744|PDB:1O7O, ECO:0007744|PDB:1O7Q, ECO:0007744|PDB:1VZT, ECO:0007744|PDB:1VZU, ECO:0007744|PDB:1VZX, ECO:0007744|PDB:2JCK, ECO:0007744|PDB:2VFZ, ECO:0007744|PDB:2VS3, ECO:0007744|PDB:2VS4, ECO:0007744|PDB:2VS5, ECO:0007744|PDB:2VXL, ECO:0007744|PDB:2WGZ |
Chain | Residue | Details |
A | PHE134 | |
B | PHE134 | |
C | PHE134 | |
D | PHE134 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11179209, ECO:0000269|PubMed:11592969, ECO:0000269|PubMed:12011052, ECO:0007744|PDB:1G8O, ECO:0007744|PDB:1G93, ECO:0007744|PDB:1GWV, ECO:0007744|PDB:1GWW, ECO:0007744|PDB:1GX0, ECO:0007744|PDB:1GX4, ECO:0007744|PDB:1K4V, ECO:0007744|PDB:1O7O, ECO:0007744|PDB:1O7Q, ECO:0007744|PDB:1VZT, ECO:0007744|PDB:1VZU, ECO:0007744|PDB:1VZX, ECO:0007744|PDB:2JCK, ECO:0007744|PDB:2VFZ, ECO:0007744|PDB:2VS3, ECO:0007744|PDB:2VS4, ECO:0007744|PDB:2VS5, ECO:0007744|PDB:2VXL, ECO:0007744|PDB:2WGZ |
Chain | Residue | Details |
A | ASP225 | |
A | ASP227 | |
B | ASP225 | |
B | ASP227 | |
C | ASP225 | |
C | ASP227 | |
D | ASP225 | |
D | ASP227 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12011052, ECO:0007744|PDB:1GWV, ECO:0007744|PDB:1GX4, ECO:0007744|PDB:1O7O, ECO:0007744|PDB:1O7Q, ECO:0007744|PDB:1VZX, ECO:0007744|PDB:2VS4, ECO:0007744|PDB:2WGZ |
Chain | Residue | Details |
A | GLN247 | |
A | THR259 | |
B | GLN247 | |
B | THR259 | |
C | GLN247 | |
C | THR259 | |
D | GLN247 | |
D | THR259 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN293 | |
B | ASN293 | |
C | ASN293 | |
D | ASN293 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1g8o |
Chain | Residue | Details |
A | GLU317 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1g8o |
Chain | Residue | Details |
B | GLU317 |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1g8o |
Chain | Residue | Details |
C | GLU317 |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1g8o |
Chain | Residue | Details |
D | GLU317 |
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 356 |
Chain | Residue | Details |
A | GLN247 | electrostatic stabiliser, hydrogen bond donor |
A | ARG280 | electrostatic stabiliser, hydrogen bond donor |
A | TRP314 | electrostatic stabiliser, hydrogen bond donor |
A | GLU317 | activator, covalently attached, electrostatic stabiliser, nucleofuge, nucleophile |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 356 |
Chain | Residue | Details |
B | GLN247 | electrostatic stabiliser, hydrogen bond donor |
B | ARG280 | electrostatic stabiliser, hydrogen bond donor |
B | TRP314 | electrostatic stabiliser, hydrogen bond donor |
B | GLU317 | activator, covalently attached, electrostatic stabiliser, nucleofuge, nucleophile |
site_id | MCSA3 |
Number of Residues | 4 |
Details | M-CSA 356 |
Chain | Residue | Details |
C | GLN247 | electrostatic stabiliser, hydrogen bond donor |
C | ARG280 | electrostatic stabiliser, hydrogen bond donor |
C | TRP314 | electrostatic stabiliser, hydrogen bond donor |
C | GLU317 | activator, covalently attached, electrostatic stabiliser, nucleofuge, nucleophile |
site_id | MCSA4 |
Number of Residues | 4 |
Details | M-CSA 356 |
Chain | Residue | Details |
D | GLN247 | electrostatic stabiliser, hydrogen bond donor |
D | ARG280 | electrostatic stabiliser, hydrogen bond donor |
D | TRP314 | electrostatic stabiliser, hydrogen bond donor |
D | GLU317 | activator, covalently attached, electrostatic stabiliser, nucleofuge, nucleophile |