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(-) Description

Title :  XENOPUS LAEVIS EMBRYONIC EPIDERMAL LECTIN IN COMPLEX WITH GLYCEROL PHOSPHATE
 
Authors :  K. Wangkanont, L. L. Kiessling, K. T. Forest
Date :  10 Oct 14  (Deposition) - 20 Jan 16  (Release) - 23 Mar 16  (Revision)
Method :  X-RAY DIFFRACTION
Resolution :  2.20
Chains :  Asym. Unit :  A
Biol. Unit 1:  A  (3x)
Keywords :  Lectin, Carbohydrate-Binding Protein, Calcium, Trimer, Fibrinogen- Like Domain, X-Type Lectin, Innate Immunity, Glycerol Phosphate, Microbial Epitope, Sugar Binding Protein (Keyword Search: [Gene Ontology, PubMed, Web (Google))
 
Reference :  K. Wangkanont, D. A. Wesener, J. A. Vidani, L. L. Kiessling, K. T. Fores
Structures Of Xenopus Embryonic Epidermal Lectin Reveal A Conserved Mechanism Of Microbial Glycan Recognition.
J. Biol. Chem. V. 291 5596 2016
PubMed-ID: 26755729  |  Reference-DOI: 10.1074/JBC.M115.709212

(-) Compounds

Molecule 1 - XEEL PROTEIN
    ChainsA
    EngineeredYES
    Expression SystemTRICHOPLUSIA NI
    Expression System PlasmidPFASTBAC1
    Expression System StrainHIGH FIVE
    Expression System Taxid7111
    Expression System Vector TypeBACULOVIRUS
    FragmentCARBOHYDRATE-BINDING DOMAIN
    GeneXEEL
    Organism CommonAFRICAN CLAWED FROG
    Organism ScientificXENOPUS LAEVIS
    Organism Taxid8355

 Structural Features

(-) Chains, Units

  1
Asymmetric Unit A
Biological Unit 1 (3x)A

Summary Information (see also Sequences/Alignments below)

(-) Ligands, Modified Residues, Ions  (4, 9)

Asymmetric Unit (4, 9)
No.NameCountTypeFull Name
11PE4Ligand/IonPENTAETHYLENE GLYCOL
2CA3Ligand/IonCALCIUM ION
3G3P1Ligand/IonSN-GLYCEROL-3-PHOSPHATE
4PO41Ligand/IonPHOSPHATE ION
Biological Unit 1 (3, 18)
No.NameCountTypeFull Name
11PE12Ligand/IonPENTAETHYLENE GLYCOL
2CA-1Ligand/IonCALCIUM ION
3G3P3Ligand/IonSN-GLYCEROL-3-PHOSPHATE
4PO43Ligand/IonPHOSPHATE ION

(-) Sites  (9, 9)

Asymmetric Unit (9, 9)
No.NameEvidenceResiduesDescription
1AC1SOFTWAREGLU A:116 , ASN A:118 , GLY A:121 , ASP A:127 , HOH A:530 , HOH A:570binding site for residue CA A 401
2AC2SOFTWAREHIS A:115 , GLY A:126 , ASP A:162 , ASP A:311 , HOH A:559 , HOH A:576binding site for residue CA A 402
3AC3SOFTWAREASN A:289 , GLU A:291 , GLU A:303 , G3P A:409 , HOH A:580 , HOH A:588binding site for residue CA A 403
4AC4SOFTWAREARG A:191 , ARG A:197 , HOH A:630binding site for residue PO4 A 404
5AC5SOFTWAREGLU A:141 , LYS A:222 , ASP A:224 , ILE A:225 , HOH A:636binding site for residue 1PE A 405
6AC6SOFTWARELYS A:227 , ASP A:231 , PHE A:260 , THR A:261 , LYS A:286 , HOH A:502 , HOH A:503 , HOH A:642binding site for residue 1PE A 406
7AC7SOFTWAREASP A:241 , LEU A:242 , GLY A:243 , LYS A:247binding site for residue 1PE A 407
8AC8SOFTWAREPHE A:120 , LYS A:122 , ARG A:307 , ASP A:316 , HOH A:639binding site for residue 1PE A 408
9AC9SOFTWARESER A:78 , ASN A:289 , GLU A:291 , HIS A:292 , GLU A:303 , TRP A:326 , CA A:403 , HOH A:542 , HOH A:588 , HOH A:624binding site for residue G3P A 409

(-) SS Bonds  (4, 4)

Asymmetric Unit
No.Residues
1A:70 -A:99
2A:123 -A:309
3A:228 -A:288
4A:280 -A:294

(-) Cis Peptide Bonds  (1, 1)

Asymmetric Unit
No.Residues
1Ser A:305 -Pro A:306

 Sequence-Structure Mapping

(-) SAPs(SNPs)/Variants  (0, 0)

(no "SAP(SNP)/Variant" information available for 4WN0)

(-) PROSITE Motifs  (0, 0)

(no "PROSITE Motif" information available for 4WN0)

(-) Exons   (0, 0)

(no "Exon" information available for 4WN0)

(-) Sequences/Alignments

Asymmetric Unit
   Reformat: Number of residues per line =  ('0' or empty: single-line sequence representation)
  Number of residues per labelling interval =   
  UniProt sequence: complete  aligned part    
   Show mapping: SCOP domains CATH domains Pfam domains Secondary structure (by author)
SAPs(SNPs) PROSITE motifs Exons
(details for a mapped element are shown in a popup box when the mouse pointer rests over it)
Chain A from PDB  Type:PROTEIN  Length:277
                                                                                                                                                                                                                                                                                                                     
               SCOP domains ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- SCOP domains
               CATH domains ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- CATH domains
               Pfam domains ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- Pfam domains
         Sec.struct. author ...hhhhhhhhh.....eeeeee.....eeeeeee.hhhhh.eeeeeee.............................hhhhh.....hhhhh....ee.hhhhhh...eeeeeeee...hhhhhhhhh.eeee...hhhhhhh.hhhhhhhhh...............eee.eeee.hhhhhhhhhhhhhhh.eeeeeeeeeee.....eeeeeeeeee...hhhhh.eee...............................hhhhhheeeeeeee Sec.struct. author
                 SAPs(SNPs) ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- SAPs(SNPs)
                    PROSITE ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- PROSITE
                 Transcript ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- Transcript
                 4wn0 A  66 GYRSCNEIKSSDSRAPDGIYTLATEDGESYQTFCDMTTNGGGWTLVASVHENNMFGKCTVGDRWSTQQGNMLQNPEGDGNWANYATFGLPEGATSDDYKNPGYYDIEAKNLALWHVPNKTPMVMWRNSSILRYRTQNGFLTEEGGNLFELYKKYPVKYDIGKCLADNGPAVPVVYDLGSAEKTASLYSPNGRSEFTPGFVQFRAVNSERATLALCAGVKVKGCNVEHHCIGGGGYIPEGSPRQCGDFAALDWDGYGTNLGWSASKQIIEAAVMLFYR 342
                                    75        85        95       105       115       125       135       145       155       165       175       185       195       205       215       225       235       245       255       265       275       285       295       305       315       325       335       

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  extra numbering lines below/above indicate numbering irregularities and modified residue names etc., number ends below/above '|'

 Classification and Annotation

(-) SCOP Domains  (0, 0)

(no "SCOP Domain" information available for 4WN0)

(-) CATH Domains  (0, 0)

(no "CATH Domain" information available for 4WN0)

(-) Pfam Domains  (0, 0)

(no "Pfam Domain" information available for 4WN0)

(-) Gene Ontology  (0, 0)

Asymmetric Unit(hide GO term definitions)
    (no "Gene Ontology" information available for 4WN0)

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 Related Entries

(-) Entries Sharing at Least One Protein Chain (UniProt ID)

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        ITLN1_XENLA | Q5PPM04wmo

(-) Related Entries Specified in the PDB File

4wmo