2WFA
Structure of Beta-Phosphoglucomutase inhibited with Beryllium trifluoride, in an open conformation.
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 1222 |
Chain | Residue |
A | ASP8 |
A | ASP10 |
A | ASP170 |
A | BEF1223 |
A | HOH2152 |
A | HOH2154 |
site_id | AC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE BEF A 1223 |
Chain | Residue |
A | SER114 |
A | ALA115 |
A | LYS145 |
A | MG1222 |
A | HOH2106 |
A | HOH2139 |
A | HOH2152 |
A | HOH2154 |
A | ASP8 |
A | LEU9 |
A | ASP10 |
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 | 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 |