6H8Z
T16A variant of beta-phosphoglucomutase from Lactococcus lactis in an open conformer complexed with magnesium trifluoride to 1.6 A.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 301 |
| Chain | Residue |
| A | ASP8 |
| A | ASP10 |
| A | ASP170 |
| A | MGF302 |
| A | HOH433 |
| A | HOH438 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue MGF A 302 |
| Chain | Residue |
| A | SER114 |
| A | ALA115 |
| A | LYS145 |
| A | MG301 |
| A | HOH433 |
| A | HOH438 |
| A | HOH467 |
| A | ASP8 |
| A | LEU9 |
| A | ASP10 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 303 |
| Chain | Residue |
| A | LYS74 |
| A | THR129 |
| A | PHE132 |
| A | ASP133 |
| A | ALA134 |
| A | ILE135 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Nucleophile => ECO:0000305|PubMed:15996095, ECO:0000305|PubMed:19154134 |
| Chain | Residue | Details |
| A | ASP8 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:15996095, ECO:0000305|PubMed:19154134 |
| Chain | Residue | Details |
| A | ASP10 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12081483, ECO:0000269|PubMed:12637673, ECO:0000269|PubMed:15826149, ECO:0000269|PubMed:15996095, ECO:0000269|PubMed:20164409, ECO:0007744|PDB:1LVH, ECO:0007744|PDB:1O03, ECO:0007744|PDB:1O08, ECO:0007744|PDB:1Z4N, ECO:0007744|PDB:1Z4O, ECO:0007744|PDB:1ZOL, ECO:0007744|PDB:2WF5, ECO:0007744|PDB:2WF6, ECO:0007744|PDB:2WHE |
| Chain | Residue | Details |
| A | ASP8 | |
| A | ASP10 | |
| A | ASP170 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20164409, ECO:0000305|PubMed:12637673, ECO:0007744|PDB:1O03, ECO:0007744|PDB:1O08, ECO:0007744|PDB:2WF5, ECO:0007744|PDB:2WF6 |
| Chain | Residue | Details |
| A | GLY46 | |
| A | VAL47 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20164409, ECO:0000305|PubMed:12637673, ECO:0000305|PubMed:15826149, ECO:0007744|PDB:1O03, ECO:0007744|PDB:1O08, ECO:0007744|PDB:1Z4N, ECO:0007744|PDB:1Z4O, ECO:0007744|PDB:2WF5, ECO:0007744|PDB:2WF6 |
| Chain | Residue | Details |
| A | ARG49 | |
| A | SER116 | |
| A | LYS117 | |
| A | ASN118 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| 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 |
| A | SER114 | |
| A | LYS145 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: 4-aspartylphosphate => ECO:0000269|PubMed:15996095, ECO:0000269|PubMed:19154134 |
| Chain | Residue | Details |
| A | 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 | ASP170 | metal ligand |
| A | LEU9 | electrostatic stabiliser, hydrogen bond donor |
| A | ASP10 | metal ligand, proton acceptor, proton donor |
| A | ALA16 | 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 |
