2FKF
Phosphomannomutase/Phosphoglucomutase from Pseudomonas aeruginosa with alpha-D-glucose 1,6-bisphosphate bound
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004614 | molecular_function | phosphoglucomutase activity |
| A | 0004615 | molecular_function | phosphomannomutase activity |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| A | 0009243 | biological_process | O antigen biosynthetic process |
| A | 0009244 | biological_process | lipopolysaccharide core region biosynthetic process |
| A | 0009298 | biological_process | GDP-mannose biosynthetic process |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0016868 | molecular_function | intramolecular phosphotransferase activity |
| A | 0042121 | biological_process | alginic acid biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PROSITE/UniProt
| site_id | PS00710 |
| Number of Residues | 10 |
| Details | PGM_PMM Phosphoglucomutase and phosphomannomutase phosphoserine signature. GVmLTGSHNP |
| Chain | Residue | Details |
| A | GLY102-PRO111 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:23517223 |
| Chain | Residue | Details |
| A | GLY21 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Non-phosphorylated intermediate => ECO:0000305|PubMed:11839312, ECO:0000305|PubMed:14725765, ECO:0000305|PubMed:16880541 |
| Chain | Residue | Details |
| A | HIS109 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:23517223 |
| Chain | Residue | Details |
| A | VAL330 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:14725765, ECO:0007744|PDB:1PCJ |
| Chain | Residue | Details |
| A | ASP18 | |
| A | SER309 | |
| A | MET326 | |
| A | ALA422 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | BINDING: via phosphate group => ECO:0000269|PubMed:11839312, ECO:0000269|PubMed:14725765, ECO:0000269|PubMed:16595672, ECO:0000269|PubMed:16880541, ECO:0000269|PubMed:18690721, ECO:0000269|PubMed:23517223 |
| Chain | Residue | Details |
| A | HIS109 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11839312, ECO:0000269|PubMed:14725765, ECO:0000269|PubMed:16595672, ECO:0000269|PubMed:16880541, ECO:0000269|PubMed:18690721, ECO:0000269|PubMed:22242625, ECO:0000269|PubMed:23517223, ECO:0000269|PubMed:24403075 |
| Chain | Residue | Details |
| A | GLY243 | |
| A | GLY245 | |
| A | ARG247 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:14725765, ECO:0000269|PubMed:18690721, ECO:0007744|PDB:1P5D, ECO:0007744|PDB:3BKQ |
| Chain | Residue | Details |
| A | CYS286 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:11839312, ECO:0000269|PubMed:14725765, ECO:0000269|PubMed:16595672, ECO:0000269|PubMed:16880541 |
| Chain | Residue | Details |
| A | HIS109 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1p5d |
| Chain | Residue | Details |
| A | LYS118 | |
| A | HIS109 | |
| A | HIS329 | |
| A | ARG20 | |
| A | ARG247 |
| site_id | MCSA1 |
| Number of Residues | 9 |
| Details | M-CSA 194 |
| Chain | Residue | Details |
| A | GLY21 | electrostatic stabiliser, hydrogen bond donor |
| A | HIS109 | metal ligand, nucleofuge, nucleophile |
| A | ASN110 | electrostatic stabiliser, hydrogen bond donor |
| A | ILE119 | electrostatic stabiliser, hydrogen bond donor |
| A | GLY243 | metal ligand |
| A | GLY245 | metal ligand |
| A | ARG247 | metal ligand |
| A | VAL248 | electrostatic stabiliser, hydrogen bond donor |
| A | VAL330 | electrostatic stabiliser, polar interaction |
