5OJZ
D10N variant of beta-phosphoglucomutase from Lactococcus lactis inhibited by a beryllium triflouride phosphoenzyme analogue to 1.3A resolution.
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 301 |
| Chain | Residue |
| A | ASP8 |
| A | ASN10 |
| A | ASP170 |
| A | BEF303 |
| A | HOH432 |
| A | HOH517 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 302 |
| Chain | Residue |
| A | HOH638 |
| A | HOH643 |
| A | HOH644 |
| A | HOH439 |
| A | HOH585 |
| A | HOH629 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | binding site for residue BEF A 303 |
| Chain | Residue |
| A | ASP8 |
| A | LEU9 |
| A | ASN10 |
| A | SER114 |
| A | ALA115 |
| A | LYS145 |
| A | MG301 |
| A | HOH432 |
| A | HOH517 |
| A | HOH588 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 304 |
| Chain | Residue |
| A | SER163 |
| A | GLY182 |
| A | LYS219 |
| A | HOH491 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 305 |
| Chain | Residue |
| A | GLN54 |
| A | HIS206 |
| A | HOH452 |
| A | HOH509 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 306 |
| Chain | Residue |
| A | PHE132 |
| A | ASP133 |
| A | HOH468 |
| A | HOH485 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 307 |
| Chain | Residue |
| A | MET1 |
| A | GLU140 |
| A | TRP216 |
| A | LEU217 |
| A | GLN220 |
| A | EDO308 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 308 |
| Chain | Residue |
| A | MET1 |
| A | ASP137 |
| A | TRP216 |
| A | EDO307 |
| A | HOH575 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 309 |
| Chain | Residue |
| A | GLU18 |
| A | ARG38 |
| A | LYS45 |
| A | HOH421 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 310 |
| Chain | Residue |
| A | GLU29 |
| A | ILE33 |
| A | ASN34 |
| A | GLY35 |
| A | VAL36 |
| A | HOH436 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 311 |
| Chain | Residue |
| A | ALA115 |
| A | SER144 |
| A | LYS145 |
| A | HOH407 |
| A | HOH423 |
| A | HOH427 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 312 |
| Chain | Residue |
| A | TYR93 |
| A | PRO94 |
| A | ASP203 |
| A | THR204 |
| A | HOH401 |
| A | HOH415 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 313 |
| Chain | Residue |
| A | ASP58 |
| A | ASP61 |
| A | SER88 |
| A | PRO89 |
| A | ALA90 |
| A | HOH628 |
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 | ASN10 |
| 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 | ASN10 | |
| 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 | 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 |
