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6IAV

CO-AZURIN FROM PSEUDOMONAS AERUGINOSA TREATED WITH HYDROSULFIDE

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0005515molecular_functionprotein binding
A0008270molecular_functionzinc ion binding
A0009055molecular_functionelectron transfer activity
A0042597cellular_componentperiplasmic space
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0046914molecular_functiontransition metal ion binding
B0005507molecular_functioncopper ion binding
B0005515molecular_functionprotein binding
B0008270molecular_functionzinc ion binding
B0009055molecular_functionelectron transfer activity
B0042597cellular_componentperiplasmic space
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
B0046914molecular_functiontransition metal ion binding
C0005507molecular_functioncopper ion binding
C0005515molecular_functionprotein binding
C0008270molecular_functionzinc ion binding
C0009055molecular_functionelectron transfer activity
C0042597cellular_componentperiplasmic space
C0042802molecular_functionidentical protein binding
C0046872molecular_functionmetal ion binding
C0046914molecular_functiontransition metal ion binding
D0005507molecular_functioncopper ion binding
D0005515molecular_functionprotein binding
D0008270molecular_functionzinc ion binding
D0009055molecular_functionelectron transfer activity
D0042597cellular_componentperiplasmic space
D0042802molecular_functionidentical protein binding
D0046872molecular_functionmetal ion binding
D0046914molecular_functiontransition metal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue CO A 201
ChainResidue
AGLY45
AHIS46
ACYS112
AHIS117
AMET121

site_idAC2
Number of Residues3
Detailsbinding site for residue CA A 202
ChainResidue
AASP93
ASER94
CGLY105

site_idAC3
Number of Residues5
Detailsbinding site for residue CO B 201
ChainResidue
BHIS46
BCYS112
BHIS117
BMET121
BGLY45

site_idAC4
Number of Residues3
Detailsbinding site for residue CA B 202
ChainResidue
BASP93
BSER94
DGLY105

site_idAC5
Number of Residues6
Detailsbinding site for residue CO C 201
ChainResidue
CGLY45
CHIS46
CCYS112
CPHE114
CHIS117
CMET121

site_idAC6
Number of Residues3
Detailsbinding site for residue CA C 202
ChainResidue
AGLY105
CASP93
CSER94

site_idAC7
Number of Residues5
Detailsbinding site for residue CO D 201
ChainResidue
DGLY45
DHIS46
DCYS112
DHIS117
DMET121

Functional Information from PROSITE/UniProt
site_idPS00196
Number of Residues17
DetailsCOPPER_BLUE Type-1 copper (blue) proteins signature. GeqYmFFCtfPgHsal.M
ChainResidueDetails
AGLY105-MET121

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:1420141
ChainResidueDetails
AHIS46
DHIS46
DCYS112
DHIS117
ACYS112
AHIS117
BHIS46
BCYS112
BHIS117
CHIS46
CCYS112
CHIS117

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING:
ChainResidueDetails
AMET121
BMET121
CMET121
DMET121

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PDB entries from 2024-08-21

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