6HDH
R49K variant of beta-phosphoglucomutase from Lactococcus lactis in an open conformer to 1.6 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 | 5 |
| Details | binding site for residue MG A 301 |
| Chain | Residue |
| A | ASP8 |
| A | ASP10 |
| A | GLU169 |
| A | ASP170 |
| A | HOH487 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 302 |
| Chain | Residue |
| A | SER163 |
| A | GLY182 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 303 |
| Chain | Residue |
| A | VAL188 |
| A | ASP203 |
| A | THR204 |
| A | HOH424 |
| A | TYR93 |
| A | PRO94 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 304 |
| Chain | Residue |
| A | ALA17 |
| A | PHE21 |
| A | ARG38 |
| A | ASN41 |
| A | LYS45 |
| A | HOH431 |
| B | GLU192 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 305 |
| Chain | Residue |
| A | THR129 |
| A | PHE132 |
| A | ASP133 |
| A | ALA134 |
| A | ILE135 |
| A | HOH408 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 306 |
| Chain | Residue |
| A | ASP133 |
| A | ALA157 |
| A | HOH459 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue ACT A 307 |
| Chain | Residue |
| A | THR16 |
| A | HIS20 |
| A | HOH405 |
| A | HOH442 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 301 |
| Chain | Residue |
| B | ASP8 |
| B | ASP10 |
| B | GLU169 |
| B | ASP170 |
| B | HOH484 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 302 |
| Chain | Residue |
| B | PRO94 |
| B | ASP203 |
| B | THR204 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 303 |
| Chain | Residue |
| B | SER163 |
| B | GLY182 |
| B | TRP216 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"15996095","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19154134","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"15996095","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19154134","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12081483","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12637673","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15826149","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15996095","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20164409","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LVH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O03","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O08","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Z4N","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Z4O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ZOL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WF5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WF6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WHE","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20164409","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12637673","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1O03","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O08","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WF5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WF6","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20164409","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12637673","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15826149","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1O03","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O08","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Z4N","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Z4O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WF5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WF6","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Site: {"description":"Important for catalytic activity and assists the phosphoryl transfer reaction to Asp8 by balancing charge and orienting the reacting groups"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"4-aspartylphosphate","evidences":[{"source":"PubMed","id":"15996095","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19154134","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
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 | ASP170 | metal ligand |
| 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 |
| site_id | MCSA2 |
| Number of Residues | 10 |
| Details | M-CSA 206 |
| Chain | Residue | Details |
| B | ASP8 | metal ligand, nucleofuge, nucleophile |
| B | ASP170 | metal ligand |
| 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 |
