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3C04

Structure of the P368G mutant of PMM/PGM from P. aeruginosa

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0004614molecular_functionphosphoglucomutase activity
A0004615molecular_functionphosphomannomutase activity
A0005975biological_processcarbohydrate metabolic process
A0009103biological_processlipopolysaccharide biosynthetic process
A0009243biological_processO antigen biosynthetic process
A0009244biological_processlipopolysaccharide core region biosynthetic process
A0009298biological_processGDP-mannose biosynthetic process
A0016853molecular_functionisomerase activity
A0016868molecular_functionintramolecular phosphotransferase activity
A0042121biological_processalginic acid biosynthetic process
A0046872molecular_functionmetal ion binding
A1901137biological_processcarbohydrate derivative biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A 500
ChainResidue
AASP242
AASP244
AASP246

Functional Information from PROSITE/UniProt
site_idPS00710
Number of Residues10
DetailsPGM_PMM Phosphoglucomutase and phosphomannomutase phosphoserine signature. GVmLTGSHNP
ChainResidueDetails
AGLY102-PRO111

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues96
DetailsRegion: {"description":"Topological domain 2","evidences":[{"source":"PubMed","id":"11839312","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues104
DetailsRegion: {"description":"Topological domain 3","evidences":[{"source":"PubMed","id":"11839312","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues78
DetailsRegion: {"description":"Topological domain 4","evidences":[{"source":"PubMed","id":"11839312","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"23517223","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsActive 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"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"23517223","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"14725765","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1PCJ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsBinding 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"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues3
DetailsBinding 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"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsBinding 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"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsModified 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"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1p5d
ChainResidueDetails
ALYS118
AHIS109
AHIS329
AARG20
AARG247

site_idMCSA1
Number of Residues9
DetailsM-CSA 194
ChainResidueDetails
AARG20electrostatic stabiliser, hydrogen bond donor
ASEP108metal ligand, nucleofuge, nucleophile
AASP113electrostatic stabiliser, hydrogen bond donor
AALA122electrostatic stabiliser, hydrogen bond donor
AASP246metal ligand
AVAL248metal ligand
AVAL250metal ligand
AVAL251electrostatic stabiliser, hydrogen bond donor
ALYS333electrostatic stabiliser, polar interaction

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PDB entries from 2025-10-08

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