6H92
Phosphorylated beta-phosphoglucomutase from Lactococcus lactis in an open conformer to 2.6 A
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 PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue MG A 301 |
Chain | Residue |
A | PHD8 |
A | ASP10 |
A | GLU169 |
A | ASP170 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue NA B 301 |
Chain | Residue |
B | PHD8 |
B | ASP10 |
B | ASP170 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue UVW B 302 |
Chain | Residue |
B | LYS76 |
B | LYS117 |
B | VAL47 |
B | ARG49 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile |
Chain | Residue | Details |
A | PHD8 | |
B | PHD8 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor |
Chain | Residue | Details |
A | ASP10 | |
B | ASP10 |
site_id | SWS_FT_FI3 |
Number of Residues | 20 |
Details | BINDING: |
Chain | Residue | Details |
A | PHD8 | |
A | ASP170 | |
B | PHD8 | |
B | ASP10 | |
B | TRP24 | |
B | LEU44 | |
B | SER52 | |
B | LYS76 | |
B | SER114 | |
B | LYS145 | |
B | GLU169 | |
A | ASP10 | |
B | ASP170 | |
A | TRP24 | |
A | LEU44 | |
A | SER52 | |
A | LYS76 | |
A | SER114 | |
A | LYS145 | |
A | GLU169 |
site_id | SWS_FT_FI4 |
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_FI5 |
Number of Residues | 2 |
Details | MOD_RES: 4-aspartylphosphate => ECO:0000269|PubMed:15996095 |
Chain | Residue | Details |
A | PHD8 | |
B | PHD8 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 10 |
Details | M-CSA 206 |
Chain | Residue | Details |
A | PHD8 | 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 | PHD8 | 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 |