Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5I28

Azurin T30R1, crystal form II

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005507	molecular_function	copper ion binding
A	0005515	molecular_function	protein binding
A	0008270	molecular_function	zinc ion binding
A	0009055	molecular_function	electron transfer activity
A	0042597	cellular_component	periplasmic space
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding
A	0046914	molecular_function	transition metal ion binding
B	0005507	molecular_function	copper ion binding
B	0005515	molecular_function	protein binding
B	0008270	molecular_function	zinc ion binding
B	0009055	molecular_function	electron transfer activity
B	0042597	cellular_component	periplasmic space
B	0042802	molecular_function	identical protein binding
B	0046872	molecular_function	metal ion binding
B	0046914	molecular_function	transition metal ion binding
C	0005507	molecular_function	copper ion binding
C	0005515	molecular_function	protein binding
C	0008270	molecular_function	zinc ion binding
C	0009055	molecular_function	electron transfer activity
C	0042597	cellular_component	periplasmic space
C	0042802	molecular_function	identical protein binding
C	0046872	molecular_function	metal ion binding
C	0046914	molecular_function	transition metal ion binding
D	0005507	molecular_function	copper ion binding
D	0005515	molecular_function	protein binding
D	0008270	molecular_function	zinc ion binding
D	0009055	molecular_function	electron transfer activity
D	0042597	cellular_component	periplasmic space
D	0042802	molecular_function	identical protein binding
D	0046872	molecular_function	metal ion binding
D	0046914	molecular_function	transition metal ion binding
E	0005507	molecular_function	copper ion binding
E	0005515	molecular_function	protein binding
E	0008270	molecular_function	zinc ion binding
E	0009055	molecular_function	electron transfer activity
E	0042597	cellular_component	periplasmic space
E	0042802	molecular_function	identical protein binding
E	0046872	molecular_function	metal ion binding
E	0046914	molecular_function	transition metal ion binding
F	0005507	molecular_function	copper ion binding
F	0005515	molecular_function	protein binding
F	0008270	molecular_function	zinc ion binding
F	0009055	molecular_function	electron transfer activity
F	0042597	cellular_component	periplasmic space
F	0042802	molecular_function	identical protein binding
F	0046872	molecular_function	metal ion binding
F	0046914	molecular_function	transition metal ion binding
G	0005507	molecular_function	copper ion binding
G	0005515	molecular_function	protein binding
G	0008270	molecular_function	zinc ion binding
G	0009055	molecular_function	electron transfer activity
G	0042597	cellular_component	periplasmic space
G	0042802	molecular_function	identical protein binding
G	0046872	molecular_function	metal ion binding
G	0046914	molecular_function	transition metal ion binding
H	0005507	molecular_function	copper ion binding
H	0005515	molecular_function	protein binding
H	0008270	molecular_function	zinc ion binding
H	0009055	molecular_function	electron transfer activity
H	0042597	cellular_component	periplasmic space
H	0042802	molecular_function	identical protein binding
H	0046872	molecular_function	metal ion binding
H	0046914	molecular_function	transition metal ion binding
I	0005507	molecular_function	copper ion binding
I	0005515	molecular_function	protein binding
I	0008270	molecular_function	zinc ion binding
I	0009055	molecular_function	electron transfer activity
I	0042597	cellular_component	periplasmic space
I	0042802	molecular_function	identical protein binding
I	0046872	molecular_function	metal ion binding
I	0046914	molecular_function	transition metal ion binding
J	0005507	molecular_function	copper ion binding
J	0005515	molecular_function	protein binding
J	0008270	molecular_function	zinc ion binding
J	0009055	molecular_function	electron transfer activity
J	0042597	cellular_component	periplasmic space
J	0042802	molecular_function	identical protein binding
J	0046872	molecular_function	metal ion binding
J	0046914	molecular_function	transition metal ion binding
K	0005507	molecular_function	copper ion binding
K	0005515	molecular_function	protein binding
K	0008270	molecular_function	zinc ion binding
K	0009055	molecular_function	electron transfer activity
K	0042597	cellular_component	periplasmic space
K	0042802	molecular_function	identical protein binding
K	0046872	molecular_function	metal ion binding
K	0046914	molecular_function	transition metal ion binding
L	0005507	molecular_function	copper ion binding
L	0005515	molecular_function	protein binding
L	0008270	molecular_function	zinc ion binding
L	0009055	molecular_function	electron transfer activity
L	0042597	cellular_component	periplasmic space
L	0042802	molecular_function	identical protein binding
L	0046872	molecular_function	metal ion binding
L	0046914	molecular_function	transition metal ion binding
M	0005507	molecular_function	copper ion binding
M	0005515	molecular_function	protein binding
M	0008270	molecular_function	zinc ion binding
M	0009055	molecular_function	electron transfer activity
M	0042597	cellular_component	periplasmic space
M	0042802	molecular_function	identical protein binding
M	0046872	molecular_function	metal ion binding
M	0046914	molecular_function	transition metal ion binding
N	0005507	molecular_function	copper ion binding
N	0005515	molecular_function	protein binding
N	0008270	molecular_function	zinc ion binding
N	0009055	molecular_function	electron transfer activity
N	0042597	cellular_component	periplasmic space
N	0042802	molecular_function	identical protein binding
N	0046872	molecular_function	metal ion binding
N	0046914	molecular_function	transition metal ion binding
O	0005507	molecular_function	copper ion binding
O	0005515	molecular_function	protein binding
O	0008270	molecular_function	zinc ion binding
O	0009055	molecular_function	electron transfer activity
O	0042597	cellular_component	periplasmic space
O	0042802	molecular_function	identical protein binding
O	0046872	molecular_function	metal ion binding
O	0046914	molecular_function	transition metal ion binding
P	0005507	molecular_function	copper ion binding
P	0005515	molecular_function	protein binding
P	0008270	molecular_function	zinc ion binding
P	0009055	molecular_function	electron transfer activity
P	0042597	cellular_component	periplasmic space
P	0042802	molecular_function	identical protein binding
P	0046872	molecular_function	metal ion binding
P	0046914	molecular_function	transition metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue CU A 201

Chain	Residue
A	GLY45
A	HIS46
A	CYS112
A	HIS117
A	MET121

site_id	AC2
Number of Residues	1
Details	binding site for residue GOL A 202

Chain	Residue
A	ASP69

site_id	AC3
Number of Residues	5
Details	binding site for residue CU B 201

Chain	Residue
B	HIS117
B	MET121
B	GLY45
B	HIS46
B	CYS112

site_id	AC4
Number of Residues	5
Details	binding site for residue CU C 201

Chain	Residue
C	GLY45
C	HIS46
C	CYS112
C	HIS117
C	MET121

site_id	AC5
Number of Residues	5
Details	binding site for residue CU D 201

Chain	Residue
D	GLY45
D	HIS46
D	CYS112
D	HIS117
D	MET121

site_id	AC6
Number of Residues	6
Details	binding site for residue CU E 201

Chain	Residue
E	GLY45
E	HIS46
E	CYS112
E	PHE114
E	HIS117
E	MET121

site_id	AC7
Number of Residues	5
Details	binding site for residue CU F 201

Chain	Residue
F	GLY45
F	HIS46
F	CYS112
F	HIS117
F	MET121

site_id	AC8
Number of Residues	5
Details	binding site for residue CU G 201

Chain	Residue
G	GLY45
G	HIS46
G	CYS112
G	HIS117
G	MET121

site_id	AC9
Number of Residues	5
Details	binding site for residue CU H 201

Chain	Residue
H	GLY45
H	HIS46
H	CYS112
H	HIS117
H	MET121

site_id	AD1
Number of Residues	5
Details	binding site for residue CU I 201

Chain	Residue
I	GLY45
I	HIS46
I	CYS112
I	HIS117
I	MET121

site_id	AD2
Number of Residues	5
Details	binding site for residue CU J 201

Chain	Residue
J	GLY45
J	HIS46
J	CYS112
J	HIS117
J	MET121

site_id	AD3
Number of Residues	6
Details	binding site for residue CU K 201

Chain	Residue
K	GLY45
K	HIS46
K	CYS112
K	PHE114
K	HIS117
K	MET121

site_id	AD4
Number of Residues	5
Details	binding site for residue CU L 201

Chain	Residue
L	GLY45
L	HIS46
L	CYS112
L	HIS117
L	MET121

site_id	AD5
Number of Residues	5
Details	binding site for residue CU M 201

Chain	Residue
M	GLY45
M	HIS46
M	CYS112
M	HIS117
M	MET121

site_id	AD6
Number of Residues	5
Details	binding site for residue CU N 201

Chain	Residue
N	GLY45
N	HIS46
N	CYS112
N	HIS117
N	MET121

site_id	AD7
Number of Residues	5
Details	binding site for residue CU O 201

Chain	Residue
O	GLY45
O	HIS46
O	CYS112
O	HIS117
O	MET121

site_id	AD8
Number of Residues	5
Details	binding site for residue CU P 201

Chain	Residue
P	GLY45
P	HIS46
P	CYS112
P	HIS117
P	MET121

site_id	AD9
Number of Residues	14
Details	binding site for Di-peptide PHE B 29 and R1A B 30

Chain	Residue
B	CYS3
B	SER4
B	VAL5
B	ASP6
B	VAL22
B	GLN28
B	VAL31
B	ASN32
B	VAL95
B	THR96
B	PHE97
P	GLN28
P	R1A30
P	THR96

site_id	AE1
Number of Residues	13
Details	binding site for Di-peptide R1A B 30 and VAL B 31

Chain	Residue
B	VAL5
B	ASP6
B	PHE29
B	ASN32
B	TRP48
B	SER94
B	VAL95
B	THR96
P	GLN28
P	R1A30
P	THR96
B	CYS3
B	SER4

site_id	AE2
Number of Residues	12
Details	binding site for Di-peptide PHE C 29 and R1A C 30

Chain	Residue
A	CYS3
A	GLN28
C	CYS3
C	SER4
C	VAL5
C	ASP6
C	GLN28
C	VAL31
C	ASN32
C	VAL95
C	THR96
C	PHE97

site_id	AE3
Number of Residues	13
Details	binding site for Di-peptide R1A C 30 and VAL C 31

Chain	Residue
A	CYS3
A	GLN28
C	CYS3
C	SER4
C	VAL5
C	ASP6
C	ILE7
C	PHE29
C	ASN32
C	TRP48
C	SER94
C	VAL95
C	THR96

site_id	AE4
Number of Residues	14
Details	binding site for Di-peptide PHE D 29 and R1A D 30

Chain	Residue
D	CYS3
D	SER4
D	VAL5
D	VAL22
D	GLN28
D	VAL31
D	ASN32
D	SER94
D	VAL95
D	THR96
D	PHE97
M	CYS3
M	GLN28
M	PHE29

site_id	AE5
Number of Residues	13
Details	binding site for Di-peptide R1A D 30 and VAL D 31

Chain	Residue
D	CYS3
D	SER4
D	VAL5
D	ILE7
D	PHE29
D	ASN32
D	TRP48
D	SER94
D	VAL95
D	THR96
M	CYS3
M	GLN28
M	PHE29

site_id	AE6
Number of Residues	13
Details	binding site for Di-peptide PHE E 29 and R1A E 30

Chain	Residue
E	CYS3
E	SER4
E	VAL5
E	ASP6
E	GLN28
E	GLN28
E	VAL31
E	ASN32
E	SER94
E	VAL95
E	THR96
E	THR96
E	PHE97

site_id	AE7
Number of Residues	13
Details	binding site for Di-peptide R1A E 30 and VAL E 31

Chain	Residue
E	CYS3
E	SER4
E	VAL5
E	ASP6
E	ILE7
E	GLN28
E	PHE29
E	ASN32
E	TRP48
E	SER94
E	VAL95
E	THR96
E	THR96

site_id	AE8
Number of Residues	14
Details	binding site for Di-peptide PHE F 29 and R1A F 30

Chain	Residue
F	CYS3
F	SER4
F	VAL5
F	ASP6
F	GLN28
F	VAL31
F	ASN32
F	SER94
F	VAL95
F	THR96
F	PHE97
H	GLN28
H	PHE97
H	ASP98

site_id	AE9
Number of Residues	14
Details	binding site for Di-peptide R1A F 30 and VAL F 31

Chain	Residue
F	CYS3
F	SER4
F	VAL5
F	ASP6
F	ILE7
F	PHE29
F	ASN32
F	TRP48
F	SER94
F	VAL95
F	THR96
H	GLN28
H	PHE97
H	ASP98

site_id	AF1
Number of Residues	12
Details	binding site for Di-peptide PHE G 29 and R1A G 30

Chain	Residue
G	CYS3
G	CYS3
G	SER4
G	VAL5
G	VAL22
G	GLN28
G	GLN28
G	VAL31
G	VAL95
G	THR96
G	THR96
G	PHE97

site_id	AF2
Number of Residues	14
Details	binding site for Di-peptide R1A G 30 and VAL G 31

Chain	Residue
G	CYS3
G	CYS3
G	SER4
G	VAL5
G	ILE7
G	GLN28
G	PHE29
G	PHE29
G	ASN32
G	TRP48
G	SER94
G	VAL95
G	THR96
G	THR96

site_id	AF3
Number of Residues	13
Details	binding site for Di-peptide PHE H 29 and R1A H 30

Chain	Residue
F	CYS3
F	GLN28
F	THR96
H	CYS3
H	SER4
H	VAL5
H	ILE20
H	GLN28
H	VAL31
H	ASN32
H	VAL95
H	THR96
H	PHE97

site_id	AF4
Number of Residues	15
Details	binding site for Di-peptide R1A H 30 and VAL H 31

Chain	Residue
F	CYS3
F	GLN28
F	THR96
H	CYS3
H	SER4
H	VAL5
H	ILE7
H	GLN28
H	PHE29
H	ASN32
H	LEU33
H	TRP48
H	SER94
H	VAL95
H	THR96

site_id	AF5
Number of Residues	14
Details	binding site for Di-peptide PHE I 29 and R1A I 30

Chain	Residue
I	CYS3
I	SER4
I	VAL5
I	ILE20
I	GLN28
I	VAL31
I	VAL95
I	THR96
I	PHE97
I	VAL99
L	CYS3
L	SER4
L	GLN28
L	THR96

site_id	AF6
Number of Residues	16
Details	binding site for Di-peptide R1A I 30 and VAL I 31

Chain	Residue
I	CYS3
I	SER4
I	VAL5
I	ILE7
I	GLN28
I	PHE29
I	ASN32
I	LEU33
I	TRP48
I	SER94
I	VAL95
I	THR96
L	CYS3
L	SER4
L	GLN28
L	THR96

site_id	AF7
Number of Residues	11
Details	binding site for Di-peptide PHE J 29 and R1A J 30

Chain	Residue
J	CYS3
J	SER4
J	VAL5
J	GLN28
J	GLN28
J	VAL31
J	ASN32
J	VAL95
J	THR96
J	THR96
J	PHE97

site_id	AF8
Number of Residues	12
Details	binding site for Di-peptide R1A J 30 and VAL J 31

Chain	Residue
J	CYS3
J	SER4
J	VAL5
J	ILE7
J	GLN28
J	PHE29
J	ASN32
J	TRP48
J	SER94
J	VAL95
J	THR96
J	THR96

site_id	AF9
Number of Residues	13
Details	binding site for Di-peptide PHE K 29 and R1A K 30

Chain	Residue
K	CYS3
K	SER4
K	VAL5
K	ASP6
K	GLN28
K	GLN28
K	VAL31
K	ASN32
K	SER94
K	VAL95
K	THR96
K	THR96
K	PHE97

site_id	AG1
Number of Residues	12
Details	binding site for Di-peptide R1A K 30 and VAL K 31

Chain	Residue
K	CYS3
K	SER4
K	VAL5
K	ASP6
K	GLN28
K	PHE29
K	ASN32
K	TRP48
K	SER94
K	VAL95
K	THR96
K	THR96

site_id	AG2
Number of Residues	14
Details	binding site for Di-peptide PHE L 29 and R1A L 30

Chain	Residue
I	GLN28
I	PHE97
I	HOH331
L	CYS3
L	SER4
L	VAL5
L	VAL22
L	GLN28
L	VAL31
L	ASN32
L	SER94
L	VAL95
L	THR96
L	PHE97

site_id	AG3
Number of Residues	12
Details	binding site for Di-peptide R1A L 30 and VAL L 31

Chain	Residue
I	GLN28
I	PHE97
I	HOH331
L	CYS3
L	SER4
L	VAL5
L	PHE29
L	ASN32
L	TRP48
L	SER94
L	VAL95
L	THR96

site_id	AG4
Number of Residues	16
Details	binding site for Di-peptide PHE M 29 and R1A M 30

Chain	Residue
D	GLN28
D	R1A30
D	THR96
D	PHE97
D	ASP98
M	CYS3
M	SER4
M	VAL5
M	ASP6
M	GLN28
M	VAL31
M	ASN32
M	SER94
M	VAL95
M	THR96
M	PHE97

site_id	AG5
Number of Residues	14
Details	binding site for Di-peptide R1A M 30 and VAL M 31

Chain	Residue
D	GLN28
D	THR96
D	PHE97
D	ASP98
M	CYS3
M	SER4
M	VAL5
M	ASP6
M	ILE7
M	PHE29
M	ASN32
M	SER94
M	VAL95
M	THR96

site_id	AG6
Number of Residues	14
Details	binding site for Di-peptide PHE N 29 and R1A N 30

Chain	Residue
N	CYS3
N	SER4
N	VAL5
N	GLN28
N	VAL31
N	ASN32
N	SER94
N	VAL95
N	THR96
N	PHE97
O	CYS3
O	GLN28
O	R1A30
O	THR96

site_id	AG7
Number of Residues	15
Details	binding site for Di-peptide R1A N 30 and VAL N 31

Chain	Residue
N	CYS3
N	SER4
N	VAL5
N	ILE7
N	GLN28
N	PHE29
N	ASN32
N	TRP48
N	SER94
N	VAL95
N	THR96
O	CYS3
O	GLN28
O	R1A30
O	THR96

site_id	AG8
Number of Residues	15
Details	binding site for Di-peptide PHE O 29 and R1A O 30

Chain	Residue
N	GLN28
N	R1A30
N	THR96
N	PHE97
N	ASP98
O	CYS3
O	SER4
O	VAL5
O	ASP6
O	GLN28
O	VAL31
O	ASN32
O	VAL95
O	THR96
O	PHE97

site_id	AG9
Number of Residues	16
Details	binding site for Di-peptide R1A O 30 and VAL O 31

Chain	Residue
N	GLN28
N	R1A30
N	THR96
N	PHE97
N	ASP98
O	CYS3
O	SER4
O	VAL5
O	ASP6
O	ILE7
O	PHE29
O	ASN32
O	TRP48
O	SER94
O	VAL95
O	THR96

site_id	AH1
Number of Residues	11
Details	binding site for Di-peptide PHE P 29 and R1A P 30

Chain	Residue
B	GLN28
B	R1A30
P	CYS3
P	SER4
P	VAL5
P	GLN28
P	VAL31
P	ASN32
P	VAL95
P	THR96
P	PHE97

site_id	AH2
Number of Residues	12
Details	binding site for Di-peptide R1A P 30 and VAL P 31

Chain	Residue
B	GLN28
B	R1A30
P	CYS3
P	SER4
P	VAL5
P	ILE7
P	PHE29
P	ASN32
P	TRP48
P	SER94
P	VAL95
P	THR96

Functional Information from PROSITE/UniProt

site_id	PS00196
Number of Residues	17
Details	COPPER_BLUE Type-1 copper (blue) proteins signature. GeqYmFFCtfPgHsal.M

Chain	Residue	Details
A	GLY105-MET121

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	48
Details	BINDING: BINDING => ECO:0000269\|PubMed:1420141

Chain	Residue	Details
A	HIS46
D	HIS46
D	CYS112
D	HIS117
E	HIS46
E	CYS112
E	HIS117
F	HIS46
F	CYS112
F	HIS117
G	HIS46
A	CYS112
G	CYS112
G	HIS117
H	HIS46
H	CYS112
H	HIS117
I	HIS46
I	CYS112
I	HIS117
J	HIS46
J	CYS112
A	HIS117
J	HIS117
K	HIS46
K	CYS112
K	HIS117
L	HIS46
L	CYS112
L	HIS117
M	HIS46
M	CYS112
M	HIS117
B	HIS46
N	HIS46
N	CYS112
N	HIS117
O	HIS46
O	CYS112
O	HIS117
P	HIS46
P	CYS112
P	HIS117
B	CYS112
B	HIS117
C	HIS46
C	CYS112
C	HIS117

site_id	SWS_FT_FI2
Number of Residues	16
Details	BINDING:

Chain	Residue	Details
A	MET121
J	MET121
K	MET121
L	MET121
M	MET121
N	MET121
O	MET121
P	MET121
B	MET121
C	MET121
D	MET121
E	MET121
F	MET121
G	MET121
H	MET121
I	MET121

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)