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5B7M

Structure of perdeuterated CueO - the signal peptide was truncated by HRV3C protease

Functional Information from GO Data
ChainGOidnamespacecontents
A0004322molecular_functionferroxidase activity
A0005507molecular_functioncopper ion binding
A0010273biological_processdetoxification of copper ion
A0016491molecular_functionoxidoreductase activity
A0016682molecular_functionoxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor
A0016722molecular_functionoxidoreductase activity, acting on metal ions
A0016724molecular_functionoxidoreductase activity, acting on metal ions, oxygen as acceptor
A0030288cellular_componentouter membrane-bounded periplasmic space
A0042597cellular_componentperiplasmic space
A0046688biological_processresponse to copper ion
A0046872molecular_functionmetal ion binding
B0004322molecular_functionferroxidase activity
B0005507molecular_functioncopper ion binding
B0010273biological_processdetoxification of copper ion
B0016491molecular_functionoxidoreductase activity
B0016682molecular_functionoxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor
B0016722molecular_functionoxidoreductase activity, acting on metal ions
B0016724molecular_functionoxidoreductase activity, acting on metal ions, oxygen as acceptor
B0030288cellular_componentouter membrane-bounded periplasmic space
B0042597cellular_componentperiplasmic space
B0046688biological_processresponse to copper ion
B0046872molecular_functionmetal ion binding
C0004322molecular_functionferroxidase activity
C0005507molecular_functioncopper ion binding
C0010273biological_processdetoxification of copper ion
C0016491molecular_functionoxidoreductase activity
C0016682molecular_functionoxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor
C0016722molecular_functionoxidoreductase activity, acting on metal ions
C0016724molecular_functionoxidoreductase activity, acting on metal ions, oxygen as acceptor
C0030288cellular_componentouter membrane-bounded periplasmic space
C0042597cellular_componentperiplasmic space
C0046688biological_processresponse to copper ion
C0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue CU A 601
ChainResidue
AHIS443
ACYS500
AHIS505
AMET510

site_idAC2
Number of Residues6
Detailsbinding site for residue CU A 602
ChainResidue
AHOH936
AHIS143
AHIS446
AHIS448
AHIS499
ACU604

site_idAC3
Number of Residues5
Detailsbinding site for residue CU A 603
ChainResidue
AHIS103
ATRP139
AHIS141
AHIS501
AHOH936

site_idAC4
Number of Residues7
Detailsbinding site for residue CU A 604
ChainResidue
AHIS101
AHIS103
AHIS446
AHIS448
ACU602
AHOH798
AHOH936

site_idAC5
Number of Residues4
Detailsbinding site for residue CU B 601
ChainResidue
BHIS443
BCYS500
BHIS505
BMET510

site_idAC6
Number of Residues6
Detailsbinding site for residue CU B 602
ChainResidue
BHIS143
BHIS446
BHIS448
BHIS499
BCU604
BHOH931

site_idAC7
Number of Residues5
Detailsbinding site for residue CU B 603
ChainResidue
BHIS103
BTRP139
BHIS141
BHIS501
BHOH931

site_idAC8
Number of Residues6
Detailsbinding site for residue CU B 604
ChainResidue
BHIS101
BHIS103
BHIS446
BHIS448
BCU602
BHOH931

site_idAC9
Number of Residues4
Detailsbinding site for residue CU C 601
ChainResidue
CHIS443
CCYS500
CHIS505
CMET510

site_idAD1
Number of Residues6
Detailsbinding site for residue CU C 602
ChainResidue
CHIS143
CHIS446
CHIS448
CHIS499
CCU604
CHOH837

site_idAD2
Number of Residues6
Detailsbinding site for residue CU C 603
ChainResidue
CHIS103
CTRP139
CHIS141
CHIS501
CCU604
CHOH837

site_idAD3
Number of Residues7
Detailsbinding site for residue CU C 604
ChainResidue
CHIS101
CHIS103
CHIS446
CHIS448
CCU602
CCU603
CHOH837

Functional Information from PROSITE/UniProt
site_idPS00080
Number of Residues12
DetailsMULTICOPPER_OXIDASE2 Multicopper oxidases signature 2. HCHlleHedtGM
ChainResidueDetails
AHIS499-MET510

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: type 2 copper site => ECO:0000269|PubMed:11867755, ECO:0000269|PubMed:12794077, ECO:0000269|PubMed:17217912, ECO:0000269|PubMed:17804014, ECO:0000269|PubMed:21903583, ECO:0000269|PubMed:24598746, ECO:0007744|PDB:1KV7, ECO:0007744|PDB:1N68, ECO:0007744|PDB:1PF3, ECO:0007744|PDB:2FQE, ECO:0007744|PDB:2FQF, ECO:0007744|PDB:2FQG, ECO:0007744|PDB:2YXV, ECO:0007744|PDB:2YXW
ChainResidueDetails
AHIS101
AHIS446
BHIS101
BHIS446
CHIS101
CHIS446

site_idSWS_FT_FI2
Number of Residues18
DetailsBINDING: type 3 copper site => ECO:0000269|PubMed:11867755, ECO:0000269|PubMed:12794077, ECO:0000269|PubMed:17217912, ECO:0000269|PubMed:17804014, ECO:0000269|PubMed:21903583, ECO:0000269|PubMed:24598746, ECO:0007744|PDB:1KV7, ECO:0007744|PDB:1N68, ECO:0007744|PDB:1PF3, ECO:0007744|PDB:2FQD, ECO:0007744|PDB:2FQE, ECO:0007744|PDB:2FQF, ECO:0007744|PDB:2FQG, ECO:0007744|PDB:2YXV, ECO:0007744|PDB:2YXW
ChainResidueDetails
AHIS103
BHIS448
BHIS499
BHIS501
CHIS103
CHIS141
CHIS143
CHIS448
CHIS499
CHIS501
AHIS141
AHIS143
AHIS448
AHIS499
AHIS501
BHIS103
BHIS141
BHIS143

site_idSWS_FT_FI3
Number of Residues9
DetailsBINDING: type 1 copper site => ECO:0000269|PubMed:11867755, ECO:0000269|PubMed:12794077, ECO:0000269|PubMed:17217912, ECO:0000269|PubMed:17804014, ECO:0000269|PubMed:21903583, ECO:0000269|PubMed:24598746, ECO:0007744|PDB:1KV7, ECO:0007744|PDB:1N68, ECO:0007744|PDB:1PF3, ECO:0007744|PDB:2FQD, ECO:0007744|PDB:2FQE, ECO:0007744|PDB:2FQF, ECO:0007744|PDB:2FQG, ECO:0007744|PDB:2YXV, ECO:0007744|PDB:2YXW
ChainResidueDetails
AHIS443
ACYS500
AHIS505
BHIS443
BCYS500
BHIS505
CHIS443
CCYS500
CHIS505

218853

PDB entries from 2024-04-24

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