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(-) Description

Title :  CRYSTAL STRUCTURE OF B. SUBTILIS 168 GLPQ IN COMPLEX WITH GLYCEROL-3-PHOSPHATE (1 HOUR SOAK)
 
Authors :  F. K. K. Li, N. C. J. Strynadka
Date :  09 Sep 16  (Deposition) - 02 Nov 16  (Release) - 28 Dec 16  (Revision)
Method :  X-RAY DIFFRACTION
Resolution :  1.48
Chains :  Asym./Biol. Unit :  E
Keywords :  Hydrolase, Metal Binding Protein (Keyword Search: [Gene Ontology, PubMed, Web (Google)] )
 
Reference :  C. L. Myers, F. K. Li, B. M. Koo, O. M. El-Halfawy, S. French, C. A. Gross, N. C. Strynadka, E. D. Brown
Identification Of Two Phosphate Starvation-Induced Wall Teichoic Acid Hydrolases Provides First Insights Into The Degradative Pathway Of A Key Bacterial Cell Wall Component.
J. Biol. Chem. V. 291 26066 2016
PubMed-ID: 27780866  |  Reference-DOI: 10.1074/JBC.M116.760447

(-) Compounds

Molecule 1 - GLYCEROPHOSPHORYL DIESTER PHOSPHODIESTERASE
    Chains: E
    EC Number: 3.1.4.46
    Engineered: YES
    Expression System: ESCHERICHIA COLI BL21(DE3)
    Expression System Plasmid: PDEST17
    Expression System Taxid: 469008
    Expression System Vector Type: PLASMID
    Fragment: UNP RESIDUES 27-293
    Gene: GLPQ, YBED, BSU02130
    Organism Scientific: BACILLUS SUBTILIS
    Organism Taxid: 224308
    Strain: 168
    Synonym: GLYCEROPHOSPHODIESTER PHOSPHODIESTERASE

 Structural Features

(-) Chains, Units

  1
Asymmetric/Biological Unit : E

Summary Information (see also Sequences/Alignments below)

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

Asymmetric/Biological Unit (4, 4)
No.NameCountTypeFull Name
1CA1Ligand/IonCALCIUM ION
2G3P1Ligand/IonSN-GLYCEROL-3-PHOSPHATE
3NA1Ligand/IonSODIUM ION
4PO41Ligand/IonPHOSPHATE ION

(-) Sites  (4, 4)

Asymmetric Unit (4, 4)
No.NameEvidenceResiduesDescription
1AC1SOFTWAREGLU E:70 , ASP E:72 , GLU E:152 , G3P E:302 , HOH E:429binding site for residue CA E 301
2AC2SOFTWAREHIS E:43 , ARG E:44 , GLU E:70 , ASP E:72 , HIS E:85 , GLU E:152 , LYS E:154 , GLN E:188 , LEU E:210 , TYR E:259 , PHE E:279 , CA E:301 , HOH E:448 , HOH E:472binding site for residue G3P E 302
3AC3SOFTWAREHIS E:43 , THR E:260 , ASN E:262 , ASN E:281 , HOH E:432 , HOH E:448binding site for residue PO4 E 303
4AC4SOFTWAREASP E:90 , THR E:93 , HOH E:414 , HOH E:514 , HOH E:536 , HOH E:541binding site for residue NA E 304

(-) SS Bonds  (0, 0)

(no "SS Bond" information available for 5T9C)

(-) Cis Peptide Bonds  (1, 1)

Asymmetric/Biological Unit
No.Residues
1Tyr E:259 -Thr E:260

 Sequence-Structure Mapping

(-) SAPs(SNPs)/Variants  (0, 0)

(no "SAP(SNP)/Variant" information available for 5T9C)

(-) PROSITE Motifs  (0, 0)

(no "PROSITE Motif" information available for 5T9C)

(-) Exons   (0, 0)

(no "Exon" information available for 5T9C)

(-) Sequences/Alignments

Asymmetric/Biological 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 E from PDB  Type:PROTEIN  Length:263
                                                                                                                                                                                                                                                                                                       
               SCOP domains ----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- SCOP domains
               CATH domains ----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- CATH domains
               Pfam domains ----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- Pfam domains
         Sec.struct. author ........eeee...........hhhhhhhhhhh...eeeeeeee.....eee..............hhhhhhhhhhh....hhhhhhhhhhhhhhhhh.....hhhhhhhhhhhhh.eeeee.hhhhh.hhhhhhhhhhhhh...........eeeee.hhhhhhhhhhhh....eeeeehhhhhhh.hhhhhhhhhh...eeee.hhhhhhhhhhhhhhh..ee......hhhhhhhhhhhh..eeee.hhhhhhhhhh.. Sec.struct. author
                 SAPs(SNPs) ----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- SAPs(SNPs)
                    PROSITE ----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- PROSITE
                 Transcript ----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- Transcript
                 5t9c E  31 NLLSPDRILTVAHRGASGYVPEHTILSYETAQKMKADFIELDLQMTKDGKLIVMHDEKLDRTTNGMGWVKDHTLADIKKLDAGSWFNEAYPEKAKPQYVGLKVPTLEEVLDRFGKHANYYIETKSPDTYPGMEEKLIASLQKHKLLGKHSKPGQVIIQSFSKESLVKVHQLQPNLPTVQLLEAKQMASMTDAALEEIKTYAVGAGPDYKALNQENVRMIRSHGLLLHPYTVNNEADMHRLLDWGVTGVFTNYPDLFHKVKKGY 293
                                    40        50        60        70        80        90       100       110       120       130       140       150       160       170       180       190       200       210       220       230       240       250       260       270       280       290
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  x → Chemical Group (purple background, 'x', labelled with number + name, e.g. ACE or NH2)
  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 5T9C)

(-) CATH Domains  (0, 0)

(no "CATH Domain" information available for 5T9C)

(-) Pfam Domains  (0, 0)

(no "Pfam Domain" information available for 5T9C)

(-) Gene Ontology  (6, 6)

Asymmetric/Biological Unit(hide GO term definitions)

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  Cis Peptide Bonds
    Tyr E:259 - Thr E:260   [ RasMol ]  
 

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  5t9c
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  GLPQ_BACSU | P37965
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 Related Entries

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

UniProtKB/Swiss-Prot
        GLPQ_BACSU | P37965: 5t91 5t9b

(-) Related Entries Specified in the PDB File

5t91 5t9b