eF-site ID 1nzr-ABCD PDB Code 1nzr Chain A, B, C, D click to enlarge Title CRYSTAL STRUCTURE OF THE AZURIN MUTANT NICKEL-TRP48MET FROM PSEUDOMONAS AERUGINOSA AT 2.2 ANGSTROMS RESOLUTION Classification ELECTRON TRANSPORT (COPPER) Compound AZURIN Source Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) (AZUR_PSEAE) Sequence A:  AECSVDIQGNDQMQFNTNAITVDKSCKQFTVNLSHPGNLP KNVMGHNMVLSTAADMQGVVTDGMASGLDKDYLKPDDSRV IAHTKLIGSGEKDSVTFDVSKLKEGEQYMFFCTFPGHSAL MKGTLTLK B:  AECSVDIQGNDQMQFNTNAITVDKSCKQFTVNLSHPGNLP KNVMGHNMVLSTAADMQGVVTDGMASGLDKDYLKPDDSRV IAHTKLIGSGEKDSVTFDVSKLKEGEQYMFFCTFPGHSAL MKGTLTLK C:  AECSVDIQGNDQMQFNTNAITVDKSCKQFTVNLSHPGNLP KNVMGHNMVLSTAADMQGVVTDGMASGLDKDYLKPDDSRV IAHTKLIGSGEKDSVTFDVSKLKEGEQYMFFCTFPGHSAL MKGTLTLK D:  AECSVDIQGNDQMQFNTNAITVDKSCKQFTVNLSHPGNLP KNVMGHNMVLSTAADMQGVVTDGMASGLDKDYLKPDDSRV IAHTKLIGSGEKDSVTFDVSKLKEGEQYMFFCTFPGHSAL MKGTLTLK Description (1)  AZURIN MUTANT WITH TRP 48 REPLACED BY MET (W48M) Functional site 1) chain A residue 45 type sequence G description BINDING SITE FOR RESIDUE NI A 129 source : AC1 2) chain A residue 46 type sequence H description BINDING SITE FOR RESIDUE NI A 129 source : AC1 3) chain A residue 112 type sequence C description BINDING SITE FOR RESIDUE NI A 129 source : AC1 4) chain A residue 117 type sequence H description BINDING SITE FOR RESIDUE NI A 129 source : AC1 5) chain A residue 121 type sequence M description BINDING SITE FOR RESIDUE NI A 129 source : AC1 6) chain B residue 45 type sequence G description BINDING SITE FOR RESIDUE NI B 129 source : AC2 7) chain B residue 46 type sequence H description BINDING SITE FOR RESIDUE NI B 129 source : AC2 8) chain B residue 112 type sequence C description BINDING SITE FOR RESIDUE NI B 129 source : AC2 9) chain B residue 114 type sequence F description BINDING SITE FOR RESIDUE NI B 129 source : AC2 10) chain B residue 117 type sequence H description BINDING SITE FOR RESIDUE NI B 129 source : AC2 11) chain B residue 121 type sequence M description BINDING SITE FOR RESIDUE NI B 129 source : AC2 12) chain C residue 45 type sequence G description BINDING SITE FOR RESIDUE NI C 129 source : AC3 13) chain C residue 46 type sequence H description BINDING SITE FOR RESIDUE NI C 129 source : AC3 14) chain C residue 112 type sequence C description BINDING SITE FOR RESIDUE NI C 129 source : AC3 15) chain C residue 117 type sequence H description BINDING SITE FOR RESIDUE NI C 129 source : AC3 16) chain C residue 121 type sequence M description BINDING SITE FOR RESIDUE NI C 129 source : AC3 17) chain D residue 45 type sequence G description BINDING SITE FOR RESIDUE NI D 129 source : AC4 18) chain D residue 46 type sequence H description BINDING SITE FOR RESIDUE NI D 129 source : AC4 19) chain D residue 112 type sequence C description BINDING SITE FOR RESIDUE NI D 129 source : AC4 20) chain D residue 117 type sequence H description BINDING SITE FOR RESIDUE NI D 129 source : AC4 21) chain D residue 121 type sequence M description BINDING SITE FOR RESIDUE NI D 129 source : AC4 22) chain A residue 3 type sequence C description BINDING SITE FOR RESIDUE NO3 A 130 source : AC5 23) chain A residue 26 type sequence C description BINDING SITE FOR RESIDUE NO3 A 130 source : AC5 24) chain A residue 27 type sequence K description BINDING SITE FOR RESIDUE NO3 A 130 source : AC5 25) chain A residue 28 type sequence Q description BINDING SITE FOR RESIDUE NO3 A 130 source : AC5 26) chain B residue 40 type sequence P description BINDING SITE FOR RESIDUE NO3 A 130 source : AC5 27) chain B residue 42 type sequence N description BINDING SITE FOR RESIDUE NO3 A 130 source : AC5 28) chain D residue 68 type sequence L description BINDING SITE FOR RESIDUE NO3 A 130 source : AC5 29) chain A residue 46 type BINDING sequence H description BINDING => ECO:0000269|PubMed:1420141 source Swiss-Prot : SWS_FT_FI1 30) chain D residue 46 type BINDING sequence H description BINDING => ECO:0000269|PubMed:1420141 source Swiss-Prot : SWS_FT_FI1 31) chain D residue 112 type BINDING sequence C description BINDING => ECO:0000269|PubMed:1420141 source Swiss-Prot : SWS_FT_FI1 32) chain D residue 117 type BINDING sequence H description BINDING => ECO:0000269|PubMed:1420141 source Swiss-Prot : SWS_FT_FI1 33) chain A residue 112 type BINDING sequence C description BINDING => ECO:0000269|PubMed:1420141 source Swiss-Prot : SWS_FT_FI1 34) chain A residue 117 type BINDING sequence H description BINDING => ECO:0000269|PubMed:1420141 source Swiss-Prot : SWS_FT_FI1 35) chain B residue 46 type BINDING sequence H description BINDING => ECO:0000269|PubMed:1420141 source Swiss-Prot : SWS_FT_FI1 36) chain B residue 112 type BINDING sequence C description BINDING => ECO:0000269|PubMed:1420141 source Swiss-Prot : SWS_FT_FI1 37) chain B residue 117 type BINDING sequence H description BINDING => ECO:0000269|PubMed:1420141 source Swiss-Prot : SWS_FT_FI1 38) chain C residue 46 type BINDING sequence H description BINDING => ECO:0000269|PubMed:1420141 source Swiss-Prot : SWS_FT_FI1 39) chain C residue 112 type BINDING sequence C description BINDING => ECO:0000269|PubMed:1420141 source Swiss-Prot : SWS_FT_FI1 40) chain C residue 117 type BINDING sequence H description BINDING => ECO:0000269|PubMed:1420141 source Swiss-Prot : SWS_FT_FI1 41) chain A residue 121 type BINDING sequence M description source Swiss-Prot : SWS_FT_FI2 42) chain B residue 121 type BINDING sequence M description source Swiss-Prot : SWS_FT_FI2 43) chain C residue 121 type BINDING sequence M description source Swiss-Prot : SWS_FT_FI2 44) chain D residue 121 type BINDING sequence M description source Swiss-Prot : SWS_FT_FI2 45) chain A residue 105-121 type prosite sequence GEQYMFFCTFPGHSALM description COPPER_BLUE Type-1 copper (blue) proteins signature. GeqYmFFCtfPgHsal.M source prosite : PS00196

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