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5I26

Azurin T30R1, crystal form I

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 201
ChainResidue
AGLY45
AHIS46
ACYS112
AHIS117
AMET121

site_idAC2
Number of Residues5
Detailsbinding site for residue CU B 201
ChainResidue
BMET121
BGLY45
BHIS46
BCYS112
BHIS117

site_idAC3
Number of Residues6
Detailsbinding site for residue CU C 201
ChainResidue
CGLY45
CHIS46
CCYS112
CPHE114
CHIS117
CMET121

site_idAC4
Number of Residues5
Detailsbinding site for residue CU D 201
ChainResidue
DGLY45
DHIS46
DCYS112
DHIS117
DMET121

site_idAC5
Number of Residues12
Detailsbinding site for Di-peptide PHE B 29 and R1A B 30
ChainResidue
BCYS3
BSER4
BVAL5
BGLN28
BVAL31
BASN32
BVAL95
BTHR96
BPHE97
CSER34
CLYS92
CHOH313

site_idAC6
Number of Residues12
Detailsbinding site for Di-peptide R1A B 30 and VAL B 31
ChainResidue
BCYS3
BSER4
BVAL5
BILE7
BPHE29
BASN32
BSER94
BVAL95
BTHR96
CSER34
CLYS92
CHOH313

site_idAC7
Number of Residues16
Detailsbinding site for Di-peptide PHE C 29 and R1A C 30
ChainResidue
BGLN28
BTHR96
BPHE97
BASP98
BHOH377
CSER4
CVAL5
CILE20
CTHR21
CGLN28
CVAL31
CASN32
CSER94
CVAL95
CTHR96
CPHE97

site_idAC8
Number of Residues15
Detailsbinding site for Di-peptide R1A C 30 and VAL C 31
ChainResidue
BGLN28
BTHR96
BPHE97
BASP98
BHOH377
CVAL5
CILE7
CPHE29
CASN32
CLEU33
CTRP48
CASP93
CSER94
CVAL95
CTHR96

site_idAC9
Number of Residues12
Detailsbinding site for Di-peptide PHE D 29 and R1A D 30
ChainResidue
DCYS3
DSER4
DVAL5
DVAL22
DLYS27
DGLN28
DVAL31
DASN32
DSER94
DVAL95
DTHR96
DPHE97

site_idAD1
Number of Residues11
Detailsbinding site for Di-peptide R1A D 30 and VAL D 31
ChainResidue
DCYS3
DSER4
DVAL5
DILE7
DLYS27
DPHE29
DASN32
DTRP48
DSER94
DVAL95
DTHR96

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 site: {"evidences":[{"source":"PubMed","id":"1420141","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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