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(-) Description

Title :  HUMAN L-TYPE FERRITIN IRON LOADED FOR 60 MINUTES
 
Authors :  C. Pozzi, F. Di Pisa, S. Mangani
Date :  06 Jul 16  (Deposition) - 22 Feb 17  (Release) - 22 Mar 17  (Revision)
Method :  X-RAY DIFFRACTION
Resolution :  1.98
Chains :  Asym. Unit :  A
Biol. Unit 1:  A  (24x)
Keywords :  L-Type, Ferritin, Mineralization, Iron, Metal Binding Protein (Keyword Search: [Gene Ontology, PubMed, Web (Google))
 
Reference :  C. Pozzi, S. Ciambellotti, C. Bernacchioni, F. Di Pisa, S. Mangani, P. Turano
Chemistry At The Protein-Mineral Interface In L-Ferritin Assists The Assembly Of A Functional ( Mu (3)-Oxo)Tris[( Mu (2)-Peroxo)] Triiron(Iii) Cluster.
Proc. Natl. Acad. Sci. V. 114 2580 2017 U. S. A.
PubMed-ID: 28202724  |  Reference-DOI: 10.1073/PNAS.1614302114

(-) Compounds

Molecule 1 - FERRITIN LIGHT CHAIN
    ChainsA
    EngineeredYES
    Expression SystemESCHERICHIA COLI BL21
    Expression System PlasmidPET21C
    Expression System Taxid511693
    Expression System VariantPLYSS
    Expression System Vector TypePLASMID
    GeneFTL
    Organism CommonHUMAN
    Organism ScientificHOMO SAPIENS
    Organism Taxid9606
    SynonymFERRITIN L SUBUNIT

 Structural Features

(-) Chains, Units

  1
Asymmetric Unit A
Biological Unit 1 (24x)A

Summary Information (see also Sequences/Alignments below)

(-) Ligands, Modified Residues, Ions  (5, 17)

Asymmetric Unit (5, 17)
No.NameCountTypeFull Name
1CD8Ligand/IonCADMIUM ION
2FE4Ligand/IonFE (III) ION
3OXY1Ligand/IonOXYGEN MOLECULE
4PER3Ligand/IonPEROXIDE ION
5SO41Ligand/IonSULFATE ION
Biological Unit 1 (3, 120)
No.NameCountTypeFull Name
1CD-1Ligand/IonCADMIUM ION
2FE-1Ligand/IonFE (III) ION
3OXY24Ligand/IonOXYGEN MOLECULE
4PER72Ligand/IonPEROXIDE ION
5SO424Ligand/IonSULFATE ION

(-) Sites  (17, 17)

Asymmetric Unit (17, 17)
No.NameEvidenceResiduesDescription
01AC1SOFTWAREASP A:15 , HOH A:432 , HOH A:445binding site for residue CD A 201
02AC2SOFTWAREASP A:131binding site for residue CD A 202
03AC3SOFTWARECYS A:130 , GLU A:134binding site for residue CD A 203
04AC4SOFTWAREHIS A:118 , CYS A:130 , GLU A:134 , HOH A:484binding site for residue CD A 204
05AC5SOFTWAREHIS A:136 , HOH A:449 , HOH A:464binding site for residue CD A 205
06AC6SOFTWAREGLU A:90 , HOH A:395 , HOH A:416 , HOH A:450binding site for residue CD A 206
07AC7SOFTWAREGLU A:49 , ASP A:178binding site for residue CD A 207
08AC8SOFTWAREGLU A:90binding site for residue CD A 208
09AC9SOFTWAREGLU A:61 , GLU A:64 , FE A:210 , FE A:211 , OXY A:213 , PER A:214 , PER A:216 , HOH A:383binding site for residue FE A 209
10AD1SOFTWAREGLU A:57 , GLU A:60 , GLU A:61 , FE A:209 , FE A:211 , OXY A:213 , PER A:215 , PER A:216binding site for residue FE A 210
11AD2SOFTWAREGLU A:60 , GLU A:64 , FE A:209 , FE A:210 , OXY A:213 , PER A:214 , PER A:215 , HOH A:382binding site for residue FE A 211
12AD3SOFTWAREGLU A:57 , PER A:215 , HOH A:457 , HOH A:496binding site for residue FE A 212
13AD4SOFTWAREGLU A:60 , GLU A:61 , GLU A:64 , FE A:209 , FE A:210 , FE A:211 , PER A:214 , PER A:215 , PER A:216binding site for residue OXY A 213
14AD5SOFTWAREGLU A:64 , FE A:209 , FE A:211 , OXY A:213 , PER A:216 , HOH A:383binding site for residue PER A 214
15AD6SOFTWAREGLU A:57 , GLU A:60 , FE A:210 , FE A:211 , FE A:212 , OXY A:213 , HOH A:388binding site for residue PER A 215
16AD7SOFTWAREGLU A:57 , GLU A:61 , FE A:209 , FE A:210 , OXY A:213 , PER A:214binding site for residue PER A 216
17AD8SOFTWARESER A:13 , ASP A:15 , ARG A:124 , HOH A:318 , HOH A:327 , HOH A:364 , HOH A:415 , HOH A:432binding site for residue SO4 A 217

(-) SS Bonds  (0, 0)

(no "SS Bond" information available for 5LG8)

(-) Cis Peptide Bonds  (0, 0)

(no "Cis Peptide Bond" information available for 5LG8)

 Sequence-Structure Mapping

(-) SAPs(SNPs)/Variants  (0, 0)

(no "SAP(SNP)/Variant" information available for 5LG8)

(-) PROSITE Motifs  (0, 0)

(no "PROSITE Motif" information available for 5LG8)

(-) Exons   (0, 0)

(no "Exon" information available for 5LG8)

(-) Sequences/Alignments

Asymmetric Unit
   Reformat: Number of residues per line =  ('0' or empty: single-line sequence representation)
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  UniProt sequence: complete  aligned part    
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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:173
                                                                                                                                                                                                             
               SCOP domains ----------------------------------------------------------------------------------------------------------------------------------------------------------------------------- SCOP domains
               CATH domains ----------------------------------------------------------------------------------------------------------------------------------------------------------------------------- CATH domains
               Pfam domains ----------------------------------------------------------------------------------------------------------------------------------------------------------------------------- Pfam domains
         Sec.struct. author .......hhhhhhhhhhhhhhhhhhhhhhhhhhhhhh.....hhhhhhhhhhhhhhhhhhhhhhhhhhhhhh.................hhhhhhhhhhhhhhhhhhhhhhhhhhhhhh.hhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhh.... Sec.struct. author
                 SAPs(SNPs) ----------------------------------------------------------------------------------------------------------------------------------------------------------------------------- SAPs(SNPs)
                    PROSITE ----------------------------------------------------------------------------------------------------------------------------------------------------------------------------- PROSITE
                 Transcript ----------------------------------------------------------------------------------------------------------------------------------------------------------------------------- Transcript
                 5lg8 A   6 SQIRQNYSTDVEAAVNSLVNLYLQASYTYLSLGFYFDRDDVALEGVSHFFRELAEEKREGYERLLKMQNQRGGRALFQDIKKPAEDEWGKTPDAMKAAMALEKKLNQALLDLHALGSARTDPHLCDFLETHFLDEEVKLIKKMGDHLTNLHRLGGPEAGLGEYLFERLTLKHD 178
                                    15        25        35        45        55        65        75        85        95       105       115       125       135       145       155       165       175   

   Legend:   → Mismatch (orange background)
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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 5LG8)

(-) CATH Domains  (0, 0)

(no "CATH Domain" information available for 5LG8)

(-) Pfam Domains  (0, 0)

(no "Pfam Domain" information available for 5LG8)

(-) Gene Ontology  (12, 12)

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 Related Entries

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

UniProtKB/Swiss-Prot
        FRIL_HUMAN | P027922ffx 2fg4 2fg8 3kxu 4v6b

(-) Related Entries Specified in the PDB File

5lg2 HORSE L-TYPE FERRITIN IRON LOADED FOR 60 MINUTES