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3IBO

Pseudomonas aeruginosa E2Q/H83Q/T126H-azurin RE(PHEN)(CO)3

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
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
B0005886cellular_componentplasma membrane
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
C0005886cellular_componentplasma membrane
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
D0005886cellular_componentplasma membrane
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 CU A 901
ChainResidue
AGLY45
AHIS46
ACYS112
AHIS117
AMET121

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE REP A 801
ChainResidue
AHIS126
AALA19
ATHR21
AGLN107
ATHR124

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU B 901
ChainResidue
BGLY45
BHIS46
BCYS112
BHIS117
BMET121

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE REP B 801
ChainResidue
BGLN107
BTHR124
BHIS126
BHOH1461
BHOH1732
BHOH1733

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU C 901
ChainResidue
CGLY45
CHIS46
CCYS112
CHIS117
CMET121

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE REP C 801
ChainResidue
CGLY105
CGLN107
CHIS126
CLYS128
CHOH1513

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU D 901
ChainResidue
DGLY45
DHIS46
DCYS112
DHIS117
DMET121

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE REP D 801
ChainResidue
DGLN107
DTHR124
DHIS126

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 Residues508
DetailsDomain: {"description":"Plastocyanin-like"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"1420141","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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