5JQX
Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with phosphoglyceric acid (PGA) - GpgS*PGA
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0006011 | biological_process | UDP-glucose metabolic process |
A | 0016757 | molecular_function | glycosyltransferase activity |
A | 0016758 | molecular_function | hexosyltransferase activity |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0006011 | biological_process | UDP-glucose metabolic process |
B | 0016757 | molecular_function | glycosyltransferase activity |
B | 0016758 | molecular_function | hexosyltransferase activity |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0046872 | molecular_function | metal ion binding |
C | 0000287 | molecular_function | magnesium ion binding |
C | 0006011 | biological_process | UDP-glucose metabolic process |
C | 0016757 | molecular_function | glycosyltransferase activity |
C | 0016758 | molecular_function | hexosyltransferase activity |
C | 0042803 | molecular_function | protein homodimerization activity |
C | 0046872 | molecular_function | metal ion binding |
D | 0000287 | molecular_function | magnesium ion binding |
D | 0006011 | biological_process | UDP-glucose metabolic process |
D | 0016757 | molecular_function | glycosyltransferase activity |
D | 0016758 | molecular_function | hexosyltransferase activity |
D | 0042803 | molecular_function | protein homodimerization activity |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | binding site for residue 3PG A 401 |
Chain | Residue |
A | GLY182 |
A | HOH507 |
A | HOH514 |
A | GLY183 |
A | GLY184 |
A | ARG185 |
A | VAL186 |
A | THR187 |
A | HIS258 |
A | MET269 |
A | HOH505 |
site_id | AC2 |
Number of Residues | 8 |
Details | binding site for residue 3PG B 401 |
Chain | Residue |
B | GLY183 |
B | GLY184 |
B | ARG185 |
B | VAL186 |
B | THR187 |
B | HIS258 |
B | ASN260 |
B | MET269 |
site_id | AC3 |
Number of Residues | 9 |
Details | binding site for residue 3PG C 401 |
Chain | Residue |
C | GLY183 |
C | GLY184 |
C | ARG185 |
C | VAL186 |
C | THR187 |
C | HIS258 |
C | ASN260 |
C | MET269 |
C | HOH516 |
site_id | AC4 |
Number of Residues | 8 |
Details | binding site for residue 3PG D 401 |
Chain | Residue |
D | GLY182 |
D | GLY183 |
D | GLY184 |
D | ARG185 |
D | VAL186 |
D | THR187 |
D | HIS258 |
D | MET269 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 28 |
Details | BINDING: BINDING => ECO:0000269|PubMed:26136334, ECO:0007744|PDB:4Y6N, ECO:0007744|PDB:4Y6U, ECO:0007744|PDB:4Y7F, ECO:0007744|PDB:4Y7G, ECO:0007744|PDB:4Y9X |
Chain | Residue | Details |
A | PRO50 | |
B | LYS114 | |
B | ASP134 | |
B | ASP136 | |
B | TYR229 | |
B | HIS258 | |
C | PRO50 | |
C | SER81 | |
C | LYS114 | |
C | ASP134 | |
C | ASP136 | |
A | SER81 | |
C | TYR229 | |
C | HIS258 | |
D | PRO50 | |
D | SER81 | |
D | LYS114 | |
D | ASP134 | |
D | ASP136 | |
D | TYR229 | |
D | HIS258 | |
A | LYS114 | |
A | ASP134 | |
A | ASP136 | |
A | TYR229 | |
A | HIS258 | |
B | PRO50 | |
B | SER81 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:26136334, ECO:0000269|PubMed:28625787, ECO:0007744|PDB:4Y6N, ECO:0007744|PDB:4Y6U, ECO:0007744|PDB:4Y9X, ECO:0007744|PDB:5JQX |
Chain | Residue | Details |
A | GLY184 | |
B | GLY184 | |
C | GLY184 | |
D | GLY184 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:28625787, ECO:0007744|PDB:5JT0 |
Chain | Residue | Details |
A | ARG256 | |
B | ARG256 | |
C | ARG256 | |
D | ARG256 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:26136334, ECO:0007744|PDB:4Y6N, ECO:0007744|PDB:4Y6U |
Chain | Residue | Details |
A | ASN260 | |
B | ASN260 | |
C | ASN260 | |
D | ASN260 |