Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P00282

- AZUR_PSEAE

UniProt

P00282 - AZUR_PSEAE

Protein

Azurin

Gene

azu

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 2 (01 Jul 1989)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Transfers electrons from cytochrome c551 to cytochrome oxidase.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi66 – 661Copper1 Publication
    Metal bindingi132 – 1321Copper1 Publication
    Metal bindingi137 – 1371Copper1 Publication
    Metal bindingi141 – 1411Copper

    GO - Molecular functioni

    1. copper ion binding Source: PseudoCAP
    2. electron carrier activity Source: InterPro
    3. transition metal ion binding Source: PseudoCAP
    4. zinc ion binding Source: PseudoCAP

    GO - Biological processi

    1. oxidation-reduction process Source: UniProtKB-KW

    Keywords - Biological processi

    Electron transport, Transport

    Keywords - Ligandi

    Copper, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Azurin
    Gene namesi
    Name:azu
    Ordered Locus Names:PA4922
    OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
    Taxonomic identifieri208964 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
    ProteomesiUP000002438: Chromosome

    Organism-specific databases

    PseudoCAPiPA4922.

    Subcellular locationi

    GO - Cellular componenti

    1. periplasmic space Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Periplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 20202 PublicationsAdd
    BLAST
    Chaini21 – 148128AzurinPRO_0000002863Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi23 ↔ 46

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Protein-protein interaction databases

    DIPiDIP-48787N.
    MINTiMINT-8099376.
    STRINGi208964.PA4922.

    Structurei

    Secondary structure

    1
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi24 – 296
    Beta strandi31 – 333
    Beta strandi34 – 363
    Beta strandi38 – 436
    Beta strandi47 – 548
    Beta strandi57 – 593
    Helixi61 – 644
    Beta strandi69 – 724
    Turni73 – 753
    Helixi76 – 8611
    Helixi88 – 903
    Beta strandi101 – 1033
    Beta strandi112 – 1187
    Helixi119 – 1213
    Beta strandi124 – 1263
    Beta strandi128 – 1314
    Turni135 – 1406
    Beta strandi142 – 1487

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AG0X-ray2.40A/B20-148[»]
    1AZNX-ray2.60A/B/C/D21-148[»]
    1AZRX-ray2.40A/B/C/D21-148[»]
    1AZUX-ray2.70A21-148[»]
    1BEXX-ray2.30A/B21-148[»]
    1CC3X-ray1.65A/B21-148[»]
    1E5YX-ray2.00A/B/C/D21-148[»]
    1E5ZX-ray2.00A/B/C/D21-148[»]
    1E65X-ray1.85A/B/C/D21-148[»]
    1E67X-ray2.14A/B/C/D21-148[»]
    1ETJX-ray2.30A/B/C/D21-148[»]
    1EZLX-ray2.00A/B/C/D21-148[»]
    1GR7X-ray1.80A/B/C/D21-148[»]
    1I53X-ray1.80A/B21-148[»]
    1ILSX-ray2.20A/B/C/D21-148[»]
    1ILUX-ray2.30A/B/C/D/E/F/G/H/I/K/L/M21-148[»]
    1JVLX-ray2.00A/B21-148[»]
    1JVOX-ray2.75A/B/C/D/E/F/G/H/I/J/K/L21-148[»]
    1JZEX-ray1.60A21-148[»]
    1JZFX-ray1.50A21-148[»]
    1JZGX-ray1.40A21-148[»]
    1JZHX-ray1.70A21-148[»]
    1JZIX-ray1.62A/B21-148[»]
    1JZJX-ray1.80A/B21-148[»]
    1NZRX-ray2.20A/B/C/D21-148[»]
    1R1CX-ray1.90A/B/C/D21-148[»]
    1VLXX-ray1.90A/B/C/D21-148[»]
    1XB3X-ray1.50A/B21-148[»]
    1XB6X-ray1.82A/B21-148[»]
    1XB8X-ray2.00A/C21-148[»]
    2AZUX-ray1.90A/B/C/D21-148[»]
    2FNWX-ray1.40A/B21-148[»]
    2FT6X-ray1.25A21-148[»]
    2FT7X-ray1.40A21-148[»]
    2FT8X-ray1.55A21-148[»]
    2FTAX-ray1.61A/B/C/D21-148[»]
    2GHZX-ray1.60A/B21-148[»]
    2GI0X-ray1.70A/B21-148[»]
    2HX7X-ray1.55A/B21-148[»]
    2HX8X-ray1.60A/B21-148[»]
    2HX9X-ray1.70A/B21-148[»]
    2HXAX-ray2.21A/B21-148[»]
    2I7OX-ray1.50A21-148[»]
    2I7SX-ray1.35A/B/C/D21-148[»]
    2IDFX-ray2.25A/B21-148[»]
    2IWEX-ray2.83A/D/G/J21-148[»]
    2OJ1X-ray2.30A/B21-148[»]
    2TSAX-ray2.20A/B/C/D21-148[»]
    2TSBX-ray2.30A/B/C/D21-148[»]
    2XV0X-ray1.60A21-148[»]
    2XV2X-ray1.60A21-148[»]
    2XV3X-ray2.30A/B21-148[»]
    3AZUX-ray2.10A/B/C/D21-148[»]
    3FPYX-ray2.10A21-148[»]
    3FQ1X-ray1.90A21-148[»]
    3FQ2X-ray1.91A21-148[»]
    3FQYX-ray1.90A21-148[»]
    3FS9X-ray1.05A21-132[»]
    3FSAX-ray0.98A21-132[»]
    3FSVX-ray2.30A21-132[»]
    3FSWX-ray2.00A/B/C/D21-148[»]
    3FSZX-ray2.00A/B21-132[»]
    3FT0X-ray1.80A/B21-132[»]
    3IBOX-ray1.45A/B/C/D21-148[»]
    3IN0X-ray2.35A/B/C/D21-148[»]
    3IN2X-ray2.60A21-148[»]
    3JT2X-ray2.10A/B21-148[»]
    3JTBX-ray1.80A/B/C/D21-148[»]
    3N2JX-ray1.35A/B/C/D/E/F/G/H/I/J/K/L21-148[»]
    3NP3X-ray2.10A21-148[»]
    3NP4X-ray2.25A21-148[»]
    3OQRX-ray2.40A21-148[»]
    3U25X-ray1.18A/B22-148[»]
    3UGEX-ray1.70A/B/C/D21-148[»]
    4AZUX-ray1.90A/B/C/D21-148[»]
    4BWWX-ray1.48A/B/C/D21-148[»]
    4HHGX-ray1.60A21-148[»]
    4HHWX-ray2.00A/B21-148[»]
    4HIPX-ray1.90A/B21-148[»]
    4HZ1X-ray2.20A/B/C/D21-148[»]
    4JKNX-ray1.54A/B/C/D21-148[»]
    4K9JX-ray1.70A21-148[»]
    4KO5X-ray1.79A/B21-148[»]
    4KO6X-ray1.74A/B/C/D21-148[»]
    4KO7X-ray2.07A/B/C/D21-148[»]
    4KO9X-ray2.05A/B/C/D21-148[»]
    4KOBX-ray1.87A/B/C/D21-148[»]
    4KOCX-ray1.46A21-148[»]
    4MFHX-ray1.54A/B/C21-148[»]
    5AZUX-ray1.90A/B/C/D21-148[»]
    ProteinModelPortaliP00282.
    SMRiP00282. Positions 21-148.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00282.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini21 – 148128Plastocyanin-likeAdd
    BLAST

    Sequence similaritiesi

    Contains 1 plastocyanin-like domain.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3241.
    HOGENOMiHOG000280572.
    OMAiESNDAMQ.
    OrthoDBiEOG6G20MV.
    PhylomeDBiP00282.

    Family and domain databases

    Gene3Di2.60.40.420. 1 hit.
    InterProiIPR014068. Azurin_proteobac.
    IPR000923. BlueCu_1.
    IPR028871. BlueCu_1_BS.
    IPR008972. Cupredoxin.
    [Graphical view]
    PfamiPF00127. Copper-bind. 1 hit.
    [Graphical view]
    SUPFAMiSSF49503. SSF49503. 1 hit.
    TIGRFAMsiTIGR02695. azurin. 1 hit.
    PROSITEiPS00196. COPPER_BLUE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P00282-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLRKLAAVSL LSLLSAPLLA AECSVDIQGN DQMQFNTNAI TVDKSCKQFT    50
    VNLSHPGNLP KNVMGHNWVL STAADMQGVV TDGMASGLDK DYLKPDDSRV 100
    IAHTKLIGSG EKDSVTFDVS KLKEGEQYMF FCTFPGHSAL MKGTLTLK 148
    Length:148
    Mass (Da):16,008
    Last modified:July 1, 1989 - v2
    Checksum:i9C3881D7B6D64B67
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X07317 Genomic DNA. Translation: CAA30279.1.
    M30389 Genomic DNA. Translation: AAA25730.1.
    AE004091 Genomic DNA. Translation: AAG08307.1.
    PIRiJQ0644. AZPSCA.
    RefSeqiNP_253609.1. NC_002516.2.

    Genome annotation databases

    EnsemblBacteriaiAAG08307; AAG08307; PA4922.
    GeneIDi878046.
    KEGGipae:PA4922.
    PATRICi19844648. VBIPseAer58763_5155.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X07317 Genomic DNA. Translation: CAA30279.1 .
    M30389 Genomic DNA. Translation: AAA25730.1 .
    AE004091 Genomic DNA. Translation: AAG08307.1 .
    PIRi JQ0644. AZPSCA.
    RefSeqi NP_253609.1. NC_002516.2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AG0 X-ray 2.40 A/B 20-148 [» ]
    1AZN X-ray 2.60 A/B/C/D 21-148 [» ]
    1AZR X-ray 2.40 A/B/C/D 21-148 [» ]
    1AZU X-ray 2.70 A 21-148 [» ]
    1BEX X-ray 2.30 A/B 21-148 [» ]
    1CC3 X-ray 1.65 A/B 21-148 [» ]
    1E5Y X-ray 2.00 A/B/C/D 21-148 [» ]
    1E5Z X-ray 2.00 A/B/C/D 21-148 [» ]
    1E65 X-ray 1.85 A/B/C/D 21-148 [» ]
    1E67 X-ray 2.14 A/B/C/D 21-148 [» ]
    1ETJ X-ray 2.30 A/B/C/D 21-148 [» ]
    1EZL X-ray 2.00 A/B/C/D 21-148 [» ]
    1GR7 X-ray 1.80 A/B/C/D 21-148 [» ]
    1I53 X-ray 1.80 A/B 21-148 [» ]
    1ILS X-ray 2.20 A/B/C/D 21-148 [» ]
    1ILU X-ray 2.30 A/B/C/D/E/F/G/H/I/K/L/M 21-148 [» ]
    1JVL X-ray 2.00 A/B 21-148 [» ]
    1JVO X-ray 2.75 A/B/C/D/E/F/G/H/I/J/K/L 21-148 [» ]
    1JZE X-ray 1.60 A 21-148 [» ]
    1JZF X-ray 1.50 A 21-148 [» ]
    1JZG X-ray 1.40 A 21-148 [» ]
    1JZH X-ray 1.70 A 21-148 [» ]
    1JZI X-ray 1.62 A/B 21-148 [» ]
    1JZJ X-ray 1.80 A/B 21-148 [» ]
    1NZR X-ray 2.20 A/B/C/D 21-148 [» ]
    1R1C X-ray 1.90 A/B/C/D 21-148 [» ]
    1VLX X-ray 1.90 A/B/C/D 21-148 [» ]
    1XB3 X-ray 1.50 A/B 21-148 [» ]
    1XB6 X-ray 1.82 A/B 21-148 [» ]
    1XB8 X-ray 2.00 A/C 21-148 [» ]
    2AZU X-ray 1.90 A/B/C/D 21-148 [» ]
    2FNW X-ray 1.40 A/B 21-148 [» ]
    2FT6 X-ray 1.25 A 21-148 [» ]
    2FT7 X-ray 1.40 A 21-148 [» ]
    2FT8 X-ray 1.55 A 21-148 [» ]
    2FTA X-ray 1.61 A/B/C/D 21-148 [» ]
    2GHZ X-ray 1.60 A/B 21-148 [» ]
    2GI0 X-ray 1.70 A/B 21-148 [» ]
    2HX7 X-ray 1.55 A/B 21-148 [» ]
    2HX8 X-ray 1.60 A/B 21-148 [» ]
    2HX9 X-ray 1.70 A/B 21-148 [» ]
    2HXA X-ray 2.21 A/B 21-148 [» ]
    2I7O X-ray 1.50 A 21-148 [» ]
    2I7S X-ray 1.35 A/B/C/D 21-148 [» ]
    2IDF X-ray 2.25 A/B 21-148 [» ]
    2IWE X-ray 2.83 A/D/G/J 21-148 [» ]
    2OJ1 X-ray 2.30 A/B 21-148 [» ]
    2TSA X-ray 2.20 A/B/C/D 21-148 [» ]
    2TSB X-ray 2.30 A/B/C/D 21-148 [» ]
    2XV0 X-ray 1.60 A 21-148 [» ]
    2XV2 X-ray 1.60 A 21-148 [» ]
    2XV3 X-ray 2.30 A/B 21-148 [» ]
    3AZU X-ray 2.10 A/B/C/D 21-148 [» ]
    3FPY X-ray 2.10 A 21-148 [» ]
    3FQ1 X-ray 1.90 A 21-148 [» ]
    3FQ2 X-ray 1.91 A 21-148 [» ]
    3FQY X-ray 1.90 A 21-148 [» ]
    3FS9 X-ray 1.05 A 21-132 [» ]
    3FSA X-ray 0.98 A 21-132 [» ]
    3FSV X-ray 2.30 A 21-132 [» ]
    3FSW X-ray 2.00 A/B/C/D 21-148 [» ]
    3FSZ X-ray 2.00 A/B 21-132 [» ]
    3FT0 X-ray 1.80 A/B 21-132 [» ]
    3IBO X-ray 1.45 A/B/C/D 21-148 [» ]
    3IN0 X-ray 2.35 A/B/C/D 21-148 [» ]
    3IN2 X-ray 2.60 A 21-148 [» ]
    3JT2 X-ray 2.10 A/B 21-148 [» ]
    3JTB X-ray 1.80 A/B/C/D 21-148 [» ]
    3N2J X-ray 1.35 A/B/C/D/E/F/G/H/I/J/K/L 21-148 [» ]
    3NP3 X-ray 2.10 A 21-148 [» ]
    3NP4 X-ray 2.25 A 21-148 [» ]
    3OQR X-ray 2.40 A 21-148 [» ]
    3U25 X-ray 1.18 A/B 22-148 [» ]
    3UGE X-ray 1.70 A/B/C/D 21-148 [» ]
    4AZU X-ray 1.90 A/B/C/D 21-148 [» ]
    4BWW X-ray 1.48 A/B/C/D 21-148 [» ]
    4HHG X-ray 1.60 A 21-148 [» ]
    4HHW X-ray 2.00 A/B 21-148 [» ]
    4HIP X-ray 1.90 A/B 21-148 [» ]
    4HZ1 X-ray 2.20 A/B/C/D 21-148 [» ]
    4JKN X-ray 1.54 A/B/C/D 21-148 [» ]
    4K9J X-ray 1.70 A 21-148 [» ]
    4KO5 X-ray 1.79 A/B 21-148 [» ]
    4KO6 X-ray 1.74 A/B/C/D 21-148 [» ]
    4KO7 X-ray 2.07 A/B/C/D 21-148 [» ]
    4KO9 X-ray 2.05 A/B/C/D 21-148 [» ]
    4KOB X-ray 1.87 A/B/C/D 21-148 [» ]
    4KOC X-ray 1.46 A 21-148 [» ]
    4MFH X-ray 1.54 A/B/C 21-148 [» ]
    5AZU X-ray 1.90 A/B/C/D 21-148 [» ]
    ProteinModelPortali P00282.
    SMRi P00282. Positions 21-148.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-48787N.
    MINTi MINT-8099376.
    STRINGi 208964.PA4922.

    Protocols and materials databases

    DNASUi 878046.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAG08307 ; AAG08307 ; PA4922 .
    GeneIDi 878046.
    KEGGi pae:PA4922.
    PATRICi 19844648. VBIPseAer58763_5155.

    Organism-specific databases

    PseudoCAPi PA4922.

    Phylogenomic databases

    eggNOGi COG3241.
    HOGENOMi HOG000280572.
    OMAi ESNDAMQ.
    OrthoDBi EOG6G20MV.
    PhylomeDBi P00282.

    Miscellaneous databases

    EvolutionaryTracei P00282.

    Family and domain databases

    Gene3Di 2.60.40.420. 1 hit.
    InterProi IPR014068. Azurin_proteobac.
    IPR000923. BlueCu_1.
    IPR028871. BlueCu_1_BS.
    IPR008972. Cupredoxin.
    [Graphical view ]
    Pfami PF00127. Copper-bind. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49503. SSF49503. 1 hit.
    TIGRFAMsi TIGR02695. azurin. 1 hit.
    PROSITEi PS00196. COPPER_BLUE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The azurin gene from Pseudomonas aeruginosa. Cloning and characterization."
      Arvidsson R.H.A., Nordling M., Lundberg L.G.
      Eur. J. Biochem. 179:195-200(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 10145 / DSM 50071 / JCM 5962 / LMG 1242 / NBRC 12689 / NCIMB 8295 / NRRL B-771.
    2. "Isolation and sequencing of the Alcaligenes denitrificans azurin-encoding gene: comparison with the genes encoding blue copper proteins from Pseudomonas aeruginosa and Alcaligenes faecalis."
      Hoitink C.W.G., Woudt L.P., Turenhout J.C.M., van de Kamp M., Canters G.W.
      Gene 90:15-20(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The azurin gene from Pseudomonas aeruginosa codes for a pre-protein with a signal peptide. Cloning and sequencing of the azurin gene."
      Canters G.W.
      FEBS Lett. 212:168-172(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
    5. Ambler R.P.
      (In) Preverio A., Pechere J.-F., Coletti-preverio M.-A. (eds.); Developpements recents dans l'etude chimique de la structure des proteines, pp.289-305, INSERM, Paris (1971)
      Cited for: PROTEIN SEQUENCE OF 21-148.
      Strain: P6009.
    6. Charnock C.
      Submitted (APR-1996) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 21-41.
      Strain: ATCC 33352 / IATS 05.
    7. "A crystallographic model for azurin at 3-A resolution."
      Adman E.T., Stenkamp R.E., Sieker L.C., Jensen L.H.
      J. Mol. Biol. 123:35-47(1978) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS).
    8. "Structural features of azurin at 2.7-A resolution."
      Adman E.T., Jensen L.H.
      Isr. J. Chem. 21:8-13(1981)
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
    9. "Crystal structure of Pseudomonas aeruginosa apo-azurin at 1.85-A resolution."
      Nar H., Messerschmidt A., Huber R., van de Kamp M., Canters G.W.
      FEBS Lett. 306:119-124(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
    10. "X-ray crystal structure of the two site-specific mutants Ile7Ser and Phe110Ser of azurin from Pseudomonas aeruginosa."
      Hammann C., Messerschmidt A., Huber R., Nar H., Gilardi G., Canters G.W.
      J. Mol. Biol. 255:362-366(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANTS SER-27 AND SER-130.
    11. "Crystal structures of modified apo-His117Gly and apo-His46Gly mutants of Pseudomonas aeruginosa azurin."
      Hammann C., van Pouderoyen G., Nar H., Rueth F.-X.G., Messerschmidt A., Huber R., den Blaauwen T., Canters G.W.
      J. Mol. Biol. 266:357-366(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF MUTANT HIS-137.
    12. "X-ray structure determination and characterization of the Pseudomonas aeruginosa azurin mutant Met121Glu."
      Karlsson B.G., Tsai L.-C., Nar H., Sanders-Loehr J., Bonander N., Langer V., Sjoelin L.
      Biochemistry 36:4089-4095(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANT GLU-141.
    13. "Complete sequential 1H and 15N nuclear magnetic resonance assignments and solution secondary structure of the blue copper protein azurin from Pseudomonas aeruginosa."
      van de Kamp M., Canters G.W., Wijmenga S.S., Lommen A., Hilbers C.W., Nar H., Messerschmidt A., Huber R.
      Biochemistry 31:10194-10207(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.

    Entry informationi

    Entry nameiAZUR_PSEAE
    AccessioniPrimary (citable) accession number: P00282
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 137 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3