1K35
Crystal Structure of Phosphomannomutase/Phosphoglucomutase from P.aeruginosa
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| 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 |
| A | 1901137 | biological_process | carbohydrate derivative biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 500 |
| Chain | Residue |
| A | SEP108 |
| A | LYS118 |
| A | ASP242 |
| A | ASP244 |
| A | ASP246 |
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 | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"23517223","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Non-phosphorylated intermediate","evidences":[{"source":"PubMed","id":"11839312","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"14725765","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"16880541","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"23517223","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"14725765","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1PCJ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"via phosphate group","evidences":[{"source":"PubMed","id":"11839312","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14725765","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16595672","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16880541","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18690721","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23517223","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11839312","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14725765","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16595672","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16880541","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18690721","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22242625","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23517223","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24403075","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"14725765","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18690721","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1P5D","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3BKQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"11839312","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14725765","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16595672","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16880541","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
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 | ARG20 | electrostatic stabiliser, hydrogen bond donor |
| A | GLY116 | metal ligand, nucleofuge, nucleophile |
| A | VAL121 | electrostatic stabiliser, hydrogen bond donor |
| A | GLN130 | electrostatic stabiliser, hydrogen bond donor |
| A | ARG262 | metal ligand |
| A | LEU264 | metal ligand |
| A | LEU266 | metal ligand |
| A | PHE267 | electrostatic stabiliser, hydrogen bond donor |
| A | SER365 | electrostatic stabiliser, polar interaction |
