6HDI
R49A variant of beta-phosphoglucomutase from Lactococcus lactis in an open conformer to 2.0 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 |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| 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 | 6 |
| Details | binding site for residue MG A 301 |
| Chain | Residue |
| A | ASP8 |
| A | ASP10 |
| A | GLU169 |
| A | ASP170 |
| A | HOH432 |
| A | HOH484 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 302 |
| Chain | Residue |
| A | HOH466 |
| A | ALA115 |
| A | SER144 |
| A | LYS145 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 303 |
| Chain | Residue |
| A | VAL64 |
| A | SER65 |
| A | ASP86 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 304 |
| Chain | Residue |
| A | ASN127 |
| A | LEU128 |
| A | THR129 |
| A | GLY130 |
| A | TYR131 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 301 |
| Chain | Residue |
| B | ASP8 |
| B | ASP10 |
| B | GLU169 |
| B | ASP170 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 302 |
| Chain | Residue |
| B | MET1 |
| B | TRP216 |
| B | HOH423 |
| B | HOH447 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000305|PubMed:15996095, ECO:0000305|PubMed:19154134 |
| Chain | Residue | Details |
| A | ASP8 | |
| B | ASP8 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:15996095, ECO:0000305|PubMed:19154134 |
| Chain | Residue | Details |
| A | ASP10 | |
| B | ASP10 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| 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 | |
| B | ASP8 | |
| B | ASP10 | |
| B | ASP170 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| 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 | |
| B | GLY46 | |
| B | VAL47 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| 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 | ALA49 | |
| A | SER116 | |
| A | LYS117 | |
| A | ASN118 | |
| B | ALA49 | |
| B | SER116 | |
| B | LYS117 | |
| B | ASN118 |
| site_id | SWS_FT_FI6 |
| 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 |
| A | SER114 | |
| A | LYS145 | |
| B | SER114 | |
| B | LYS145 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: 4-aspartylphosphate => ECO:0000269|PubMed:15996095, ECO:0000269|PubMed:19154134 |
| 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 | 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 |
