3ZX1


Conserved Protein Domain Family
CuRO_1_McoC_like

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cd13855: CuRO_1_McoC_like 
Click on image for an interactive view with Cn3D
The first cupredoxin domain of a multicopper oxidase McoC and similar proteins
This family includes bacteria multicopper oxidases (MCOs) represented by McoC from pathogenic bacterium Campylobacter jejuni. McoC is a periplasmic multicopper oxidase, which has been characterized to be associated with copper homeostasis. McoC may also function to protect against oxidative stress as it may convert metallic ions into their less toxic form. MCOs are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. They are capable of oxidizing a vast range of substrates, varying from aromatic compunds to inorganic compounds such as metals. Most MCOs have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.
Statistics
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PSSM-Id: 259924
Aligned: 6 rows
Threshold Bit Score: 216.573
Created: 19-Nov-2012
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
trinuclear CuDomain 3Domain 2
Conserved site includes 4 residues -Click on image for an interactive view with Cn3D
Feature 1: trinuclear Cu binding site [ion binding site], 4 residue positions
Conserved feature residue pattern:H H H HClick to see conserved feature residue pattern help
Evidence:
  • Comment:Trinuclear copper site ligands are typically one or two HxH motifs that can be in the same domain/subunit or in different domains/subunits.
  • Structure:3ZX1; trinuclear copper binding site of Multicopper Oxidase From Campylobacter Jejuni
  • Comment:The trinuclear copper binding site of 3-domain MCOs is located at the interface of cupredoxin domains 1 and 3.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                                                       # #              
3ZX1_A        50 IFHATLEIKENHIELIk-gKKTLFYTYNGLv----PAPKIEVFEGDKLEILVKNKLk-EATTIHWHGVPVPPDQDGSPHD 123 Campylobacter j...
EAY63910     190 TFRATLVAQPVARPLLrgaRPTTFWQFGTGtqgpvVGPLIDVREGDTVEIRFVNKLp-QPSTIHWHGLPVPPDQDGNPSD 268 Burkholderia ce...
AAQ61305      75 ALRGCLTAAAVSLPLLpgkPATEFWAYNDSv----PGPAIELFEGETLGLRFDNRLp-QPTTVHWHGLPIPSDQDGNPHD 149 Chromobacterium...
AAK04022      73 LFTATLKAEPIKIRLAd-nKETEFWAYNGQl----PGPQIEVFEGDTVEIEFINHLp-QPSTVHWHGLDVPNEADGNPMD 146 Pasteurella mul...
NP_104662     73 LFKATLTAGSATARFAk-gLDTPILAYNGTs----PGPLIEAVEGDRVEITFANRIanEASTIHWHGMPVPADQDGNPMD 147 Mesorhizobium l...
YP_002794635  69 RFAGTLTLAETRHALLp-gEPTRLWTFNGSv----PGPLIELTAGDQVSLTLRNRLa-ESTTVHWHGLPVAPEFDGHPRQ 142 Laribacter hong...
Feature 1                                # #                    
3ZX1_A       124 pilaGEERIYRFEIPqDSAGTYWYHPHPHYTASKQVFMGLAGAFVIK 170 Campylobacter jejuni subsp. jejuni
EAY63910     269 pvapGASRVYRFTLPkGSAGTYWYHPHPHMMTAEQVFRGLAGPFVVR 315 Burkholderia cenocepacia PC184
AAQ61305     150 pvppGQGRDYRFSLPeDSAGSYWYHPHPHGHTAEQAYRGLAGVFVVK 196 Chromobacterium violaceum ATCC 12472
AAK04022     147 mvepQGKKVYRFTLPqGSAGTYWYHPHPHDHVSEQVYKGLAGTFVVK 193 Pasteurella multocida subsp. multocida str. Pm70
NP_104662    148 pvatGTDRTYSFDLPeASAGSYWYHPHPHGKTAEQVYRGLAGAFVVK 194 Mesorhizobium loti MAFF303099
YP_002794635 143 aiapGNDFVARWQLPaDWYGTYWYHPHPHGRTARQAAMGLAGAVLVR 189 Laribacter hongkongensis HLHK9

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