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1NHE

Crystal structure of Lactose synthase complex with UDP

Replaces:  1J94
Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0004461molecular_functionlactose synthase activity
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005989biological_processlactose biosynthetic process
A0032991cellular_componentprotein-containing complex
A0046872molecular_functionmetal ion binding
B0005975biological_processcarbohydrate metabolic process
B0016757molecular_functionglycosyltransferase activity
C0003796molecular_functionlysozyme activity
C0004461molecular_functionlactose synthase activity
C0005509molecular_functioncalcium ion binding
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005989biological_processlactose biosynthetic process
C0032991cellular_componentprotein-containing complex
C0046872molecular_functionmetal ion binding
D0005975biological_processcarbohydrate metabolic process
D0016757molecular_functionglycosyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 805
ChainResidue
ALYS79
AASP82
AGLU84
AASP87
AASP88
AHOH1158

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA C 806
ChainResidue
CASP87
CASP88
CHOH1160
CLYS79
CASP82
CGLU84

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE UDP B 809
ChainResidue
BPRO187
BPHE188
BARG189
BARG191
BPHE226
BASP252
BVAL253
BASP254
BLYS279
BTRP314
BMSE344
BHIS347
BASP350
BHOH962
BHOH1209

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE UDP D 810
ChainResidue
DPRO187
DPHE188
DARG189
DARG191
DPHE226
DASP252
DVAL253
DASP254
DLYS279
DTRP314
DMSE344
DASP350
DASN353
DHOH944
DHOH1096

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PG4 A 813
ChainResidue
AGLU2
APHE31
AHIS32
ATHR33
ASER34
AGLY35
BLYS279
BPHE280
BTRP314
BARG349

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PG4 C 814
ChainResidue
CPHE31
CHIS32
CTHR33
CSER34
CGLY35
CVAL42
CHOH1029
DTRP314
DARG349

Functional Information from PROSITE/UniProt
site_idPS00128
Number of Residues19
DetailsGLYCOSYL_HYDROL_F22_1 Glycosyl hydrolases family 22 (GH22) domain signature. CgisCdkLlddELdddiaC
ChainResidueDetails
ACYS73-CYS91

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING:
ChainResidueDetails
BPRO187
DPHE226
DVAL253
DASP254
DTRP314
DGLY316
DHIS347
DARG359
BPHE226
BVAL253
BASP254
BTRP314
BGLY316
BHIS347
BARG359
DPRO187

site_idSWS_FT_FI2
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN45
CASN45

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1fr8
ChainResidueDetails
BARG359
BGLU317
BASP319

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1fr8
ChainResidueDetails
DARG359
DGLU317
DASP319

site_idMCSA1
Number of Residues8
DetailsM-CSA 570
ChainResidueDetails
BASP252electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
BASP254metal ligand
BTRP314electrostatic stabiliser, hydrogen bond donor
BGLU317electrostatic stabiliser, hydrogen bond acceptor
BASP318activator, electrostatic stabiliser, proton acceptor, proton donor
BMSE344metal ligand
BHIS347metal ligand
BARG349electrostatic stabiliser, hydrogen bond donor

site_idMCSA2
Number of Residues8
DetailsM-CSA 570
ChainResidueDetails
DASP252electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
DASP254metal ligand
DTRP314electrostatic stabiliser, hydrogen bond donor
DGLU317electrostatic stabiliser, hydrogen bond acceptor
DASP318activator, electrostatic stabiliser, proton acceptor, proton donor
DMSE344metal ligand
DHIS347metal ligand
DARG349electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2024-07-31

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