8Q1C
Substrate-free D10N,P146A variant of beta-phosphoglucomutase from Lactococcus lactis
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 SwissProt/UniProt
| site_id | SWS_FT_FI2 |
| 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_FI3 |
| 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_FI4 |
| 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_FI7 |
| 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_FI8 |
| 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_FI9 |
| 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_FI10 |
| 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 | ASN10 | 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 | ASN10 | 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 |
