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1K2Y

Crystal Structure of Phosphomannomutase/Phosphoglucomutase S108A mutant from P. aeruginosa

Functional Information from GO Data
ChainGOidnamespacecontents
X0000287molecular_functionmagnesium ion binding
X0003824molecular_functioncatalytic activity
X0004614molecular_functionphosphoglucomutase activity
X0004615molecular_functionphosphomannomutase activity
X0005975biological_processcarbohydrate metabolic process
X0009103biological_processlipopolysaccharide biosynthetic process
X0009243biological_processO antigen biosynthetic process
X0009244biological_processlipopolysaccharide core region biosynthetic process
X0009298biological_processGDP-mannose biosynthetic process
X0016853molecular_functionisomerase activity
X0016868molecular_functionintramolecular phosphotransferase activity
X0042121biological_processalginic acid biosynthetic process
X0046872molecular_functionmetal ion binding
X1901137biological_processcarbohydrate derivative biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN X 500
ChainResidue
XASP242
XASP244
XASP246
XTLA999

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE TLA X 999
ChainResidue
XASP246
XARG247
XHIS308
XHIS329
XZN500
XHOH544
XHOH832
XHOH900
XALA108
XHIS109
XLYS118
XASP242
XASP244

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:23517223
ChainResidueDetails
XGLY21

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Non-phosphorylated intermediate => ECO:0000305|PubMed:11839312, ECO:0000305|PubMed:14725765, ECO:0000305|PubMed:16880541
ChainResidueDetails
XHIS109

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:23517223
ChainResidueDetails
XVAL330

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:14725765, ECO:0007744|PDB:1PCJ
ChainResidueDetails
XASP18
XSER309
XMET326
XALA422

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: 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
ChainResidueDetails
XHIS109

site_idSWS_FT_FI6
Number of Residues3
DetailsBINDING: 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
ChainResidueDetails
XGLY243
XGLY245
XARG247

site_idSWS_FT_FI7
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:14725765, ECO:0000269|PubMed:18690721, ECO:0007744|PDB:1P5D, ECO:0007744|PDB:3BKQ
ChainResidueDetails
XCYS286

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:11839312, ECO:0000269|PubMed:14725765, ECO:0000269|PubMed:16595672, ECO:0000269|PubMed:16880541
ChainResidueDetails
XHIS109

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1p5d
ChainResidueDetails
XLYS118
XHIS109
XHIS329
XARG20
XARG247

site_idMCSA1
Number of Residues9
DetailsM-CSA 194
ChainResidueDetails

237735

PDB entries from 2025-06-18

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