6HDF
D170N variant of beta-phosphoglucomutase from Lactococcus lactis in an open conformer to 1.4 A.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0008801 | molecular_function | beta-phosphoglucomutase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0008801 | molecular_function | beta-phosphoglucomutase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 301 |
| Chain | Residue |
| A | SER163 |
| A | GLY182 |
| A | LYS219 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 302 |
| Chain | Residue |
| A | ALA17 |
| A | GLU18 |
| A | ARG38 |
| A | ASN41 |
| A | HOH404 |
| B | GLU192 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 303 |
| Chain | Residue |
| A | ASP203 |
| A | THR204 |
| A | HOH412 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 304 |
| Chain | Residue |
| A | ALA115 |
| A | SER144 |
| A | LYS145 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 305 |
| Chain | Residue |
| A | SER105 |
| A | ASP149 |
| A | HOH433 |
| A | HOH441 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 306 |
| Chain | Residue |
| A | ASP8 |
| A | ASP10 |
| A | GLU169 |
| A | ASN170 |
| A | HOH517 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 301 |
| Chain | Residue |
| A | GLU192 |
| B | ALA17 |
| B | ARG38 |
| B | HOH401 |
| B | HOH404 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 302 |
| Chain | Residue |
| B | ASP51 |
| B | PRO89 |
| B | VAL92 |
| B | HOH419 |
| B | HOH428 |
| B | HOH448 |
| B | HOH481 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 303 |
| Chain | Residue |
| B | SER163 |
| B | GLY182 |
| B | LYS219 |
| site_id | AD1 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 304 |
| Chain | Residue |
| B | ARG125 |
| B | HOH445 |
| site_id | AD2 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 305 |
| Chain | Residue |
| B | ASP78 |
| B | HOH516 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue NA B 306 |
| Chain | Residue |
| B | ASP8 |
| B | ASP10 |
| B | GLU169 |
| B | ASN170 |
| B | HOH520 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile |
| Chain | Residue | Details |
| B | ASP8 | |
| A | ASP8 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor |
| Chain | Residue | Details |
| B | ASP10 | |
| A | ASP10 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | SER52 | |
| A | LYS76 | |
| A | SER114 | |
| A | LYS145 | |
| A | GLU169 | |
| A | ASN170 | |
| B | ASP8 | |
| B | ASP10 | |
| B | TRP24 | |
| B | LEU44 | |
| B | SER52 | |
| B | LYS76 | |
| B | SER114 | |
| B | LYS145 | |
| B | GLU169 | |
| B | ASN170 | |
| A | TRP24 | |
| A | LEU44 | |
| A | ASP8 | |
| A | ASP10 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | SITE: Important for catalytic activity and assists the phosphoryl transfer reaction to Asp8 by balancing charge and orienting the reacting groups |
| Chain | Residue | Details |
| B | SER114 | |
| B | LYS145 | |
| A | LYS145 | |
| A | SER114 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: 4-aspartylphosphate => ECO:0000269|PubMed:15996095 |
| Chain | Residue | Details |
| A | ASP8 | |
| B | ASP8 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 10 |
| Details | M-CSA 206 |
| Chain | Residue | Details |
| A | ASP8 | metal ligand, nucleofuge, nucleophile |
| A | LEU9 | electrostatic stabiliser, hydrogen bond donor |
| A | ASP10 | metal ligand, proton acceptor, proton donor |
| A | THR16 | electrostatic stabiliser |
| A | LYS45 | electrostatic stabiliser |
| A | SER114 | electrostatic stabiliser, hydrogen bond donor |
| A | ALA115 | electrostatic stabiliser, hydrogen bond donor |
| A | LYS145 | electrostatic stabiliser, hydrogen bond donor |
| A | GLU169 | metal ligand |
| A | ASN170 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 10 |
| Details | M-CSA 206 |
| Chain | Residue | Details |
| B | ASP8 | metal ligand, nucleofuge, nucleophile |
| B | LEU9 | electrostatic stabiliser, hydrogen bond donor |
| B | ASP10 | metal ligand, proton acceptor, proton donor |
| B | THR16 | electrostatic stabiliser |
| B | LYS45 | electrostatic stabiliser |
| B | SER114 | electrostatic stabiliser, hydrogen bond donor |
| B | ALA115 | electrostatic stabiliser, hydrogen bond donor |
| B | LYS145 | electrostatic stabiliser, hydrogen bond donor |
| B | GLU169 | metal ligand |
| B | ASN170 | metal ligand |
