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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
A0005615cellular_componentextracellular space
A0005989biological_processlactose biosynthetic process
A0032991cellular_componentprotein-containing complex
A0046872molecular_functionmetal ion binding
A0050829biological_processdefense response to Gram-negative bacterium
A0050830biological_processdefense response to Gram-positive bacterium
A0140767molecular_functionenzyme-substrate adaptor activity
B0005975biological_processcarbohydrate metabolic process
B0016757molecular_functionglycosyltransferase activity
C0003796molecular_functionlysozyme activity
C0004461molecular_functionlactose synthase activity
C0005509molecular_functioncalcium ion binding
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0005989biological_processlactose biosynthetic process
C0032991cellular_componentprotein-containing complex
C0046872molecular_functionmetal ion binding
C0050829biological_processdefense response to Gram-negative bacterium
C0050830biological_processdefense response to Gram-positive bacterium
C0140767molecular_functionenzyme-substrate adaptor activity
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 Residues244
DetailsDomain: {"description":"C-type lysozyme","evidences":[{"source":"PROSITE-ProRule","id":"PRU00680","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P00711","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues32
DetailsBinding site: {}
ChainResidueDetails

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
BHIS272electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
BSER274metal ligand
BCYS342electrostatic stabiliser, hydrogen bond donor
BILE345electrostatic stabiliser, hydrogen bond acceptor
BARG346activator, electrostatic stabiliser, proton acceptor, proton donor
BASN376metal ligand
BLEU383metal ligand
BVAL385electrostatic stabiliser, hydrogen bond donor

site_idMCSA2
Number of Residues8
DetailsM-CSA 570
ChainResidueDetails
DHIS272electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
DSER274metal ligand
DCYS342electrostatic stabiliser, hydrogen bond donor
DILE345electrostatic stabiliser, hydrogen bond acceptor
DARG346activator, electrostatic stabiliser, proton acceptor, proton donor
DASN376metal ligand
DLEU383metal ligand
DVAL385electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2025-12-03

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