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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
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
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
XGLY21electrostatic stabiliser, hydrogen bond donor
XHIS109metal ligand, nucleofuge, nucleophile
XASN110electrostatic stabiliser, hydrogen bond donor
XILE119electrostatic stabiliser, hydrogen bond donor
XGLY243metal ligand
XGLY245metal ligand
XARG247metal ligand
XVAL248electrostatic stabiliser, hydrogen bond donor
XVAL330electrostatic stabiliser, polar interaction

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PDB entries from 2024-10-30

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