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(-) Description

Title :  CRYSTAL STRUCTURE OF COPPER NITRITE REDUCTASE AT 100K AFTER 0.69 MGY
 
Authors :  S. Horrell, M. A. Hough, R. W. Strange
Date :  16 Feb 16  (Deposition) - 13 Jul 16  (Release) - 28 Sep 16  (Revision)
Method :  X-RAY DIFFRACTION
Resolution :  1.07
Chains :  Asym. Unit :  A
Biol. Unit 1:  A  (3x)
Keywords :  Copper Nitrite Reductase, Reaction Mechanism, Serial Crystallography, Oxidoreductase (Keyword Search: [Gene Ontology, PubMed, Web (Google))
 
Reference :  S. Horrell, S. V. Antonyuk, R. R. Eady, S. S. Hasnain, M. A. Hough, R. W. Strange
Serial Crystallography Captures Enzyme Catalysis In Copper Nitrite Reductase At Atomic Resolution From One Crystal.
Iucrj V. 3 271 2016
PubMed-ID: 27437114  |  Reference-DOI: 10.1107/S205225251600823X

(-) Compounds

Molecule 1 - COPPER-CONTAINING NITRITE REDUCTASE
    ChainsA
    EC Number1.7.2.1
    EngineeredYES
    Expression SystemESCHERICHIA COLI BL21(DE3)
    Expression System PlasmidPET-26B(+)
    Expression System Taxid469008
    Expression System Vector TypePLASMID
    FragmentCOPPER NITRITE REDUCTASE
    GeneNIRK
    Organism ScientificACHROMOBACTER CYCLOCLASTES
    Organism Taxid223
    SynonymCU-NIR

 Structural Features

(-) Chains, Units

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

Summary Information (see also Sequences/Alignments below)

(-) Ligands, Modified Residues, Ions  (2, 8)

Asymmetric Unit (2, 8)
No.NameCountTypeFull Name
1CU2Ligand/IonCOPPER (II) ION
2NO26Ligand/IonNITRITE ION
Biological Unit 1 (1, 18)
No.NameCountTypeFull Name
1CU-1Ligand/IonCOPPER (II) ION
2NO218Ligand/IonNITRITE ION

(-) Sites  (8, 8)

Asymmetric Unit (8, 8)
No.NameEvidenceResiduesDescription
1AC1SOFTWAREHIS A:95 , CYS A:136 , HIS A:145 , MET A:150binding site for residue CU A 501
2AC2SOFTWAREHIS A:100 , HIS A:135 , HIS A:306 , NO2 A:503 , HOH A:601binding site for residue CU A 502
3AC3SOFTWAREASP A:98 , HIS A:100 , HIS A:135 , HIS A:255 , ILE A:257 , HIS A:306 , LEU A:308 , CU A:502 , HOH A:601 , HOH A:786 , HOH A:859binding site for residue NO2 A 503
4AC4SOFTWARETRP A:265 , ALA A:266 , THR A:267 , GLY A:268 , LYS A:269 , ASN A:272 , GLN A:278 , HOH A:740 , HOH A:855binding site for residue NO2 A 504
5AC5SOFTWAREARG A:250 , ASP A:251 , ARG A:253 , ASN A:307binding site for residue NO2 A 505
6AC6SOFTWAREARG A:54 , HOH A:761 , HOH A:873binding site for residue NO2 A 506
7AC7SOFTWARETHR A:171 , ARG A:240 , HOH A:621 , HOH A:624binding site for residue NO2 A 507
8AC8SOFTWARELYS A:125 , THR A:127 , ARG A:296 , LEU A:330 , HOH A:712binding site for residue NO2 A 508

(-) SS Bonds  (0, 0)

(no "SS Bond" information available for 5I6K)

(-) Cis Peptide Bonds  (2, 2)

Asymmetric Unit
No.Residues
1Pro A:22 -Pro A:23
2Val A:68 -Pro A:69

 Sequence-Structure Mapping

(-) SAPs(SNPs)/Variants  (0, 0)

(no "SAP(SNP)/Variant" information available for 5I6K)

(-) PROSITE Motifs  (0, 0)

(no "PROSITE Motif" information available for 5I6K)

(-) Exons   (0, 0)

(no "Exon" information available for 5I6K)

(-) 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:334
                                                                                                                                                                                                                                                                                                                                                                              
               SCOP domains ---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- SCOP domains
               CATH domains ---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- CATH domains
               Pfam domains ---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- Pfam domains
         Sec.struct. author .hhhhh.eee.....................eeeeeeeeeeeeee......eeeeeee.......eeeee...eeeeeeee..........ee....hhhhhhhhh.....eeeeeeee....eeeeee.....hhhhhhhh..eeeeeee....ee.....ee...eeeeeeeeee..............hhhhhhhhhhhhhhh....eeee.......hhhhheeee...eeeeeeee......eeee...eeeee.........eeee........eeeeeeee....eeeeeee.hhhhhhh...eeeeeee................. Sec.struct. author
                 SAPs(SNPs) ---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- SAPs(SNPs)
                    PROSITE ---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- PROSITE
                 Transcript ---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- Transcript
                 5i6k A   7 VDISTLPRVKVDLVKPPFVHAHDQVAKTGPRVVEFTMTIEEKKLVIDREGTEIHAMTFNGSVPGPLMVVHENDYVELRLINPDTNTLLHNIDFHAATGALGGGALTQVNPGEETTLRFKATKPGVFVYHCAPEGMVPWHVTSGMNGAIMVLPRDGLKDEKGQPLTYDKIYYVGEQDFYVPKDEAGNYKKYETPGEAYEDAVKAMRTLTPTHIVFNGAVGALTGDHALTAAVGERVLVVHSQANRDTRPHLIGGHGDYVWATGKFRNPPDLDQETWLIPGGTAGAAFYTFRQPGVYAYVNHNLIEAFELGAAGHFKVTGEWNDDLMTSVVKPASM 340
                                    16        26        36        46        56        66        76        86        96       106       116       126       136       146       156       166       176       186       196       206       216       226       236       246       256       266       276       286       296       306       316       326       336    

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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 5I6K)

(-) CATH Domains  (0, 0)

(no "CATH Domain" information available for 5I6K)

(-) Pfam Domains  (0, 0)

(no "Pfam Domain" information available for 5I6K)

(-) Gene Ontology  (9, 9)

Asymmetric Unit(hide GO term definitions)

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 Related Entries

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

UniProtKB/Swiss-Prot
        NIR_ACHCY | P250061kcb 1nia 1nib 1nic 1nid 1nie 1nif 1rzp 1rzq 2avf 2bw4 2bw5 2bwd 2bwi 2nrd 2y1a 5akr 5i6l 5i6m 5i6n 5i6o 5i6p

(-) Related Entries Specified in the PDB File

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