1EZL

CRYSTAL STRUCTURE OF THE DISULPHIDE BOND-DEFICIENT AZURIN MUTANT C3A/C26A: HOW IMPORTANT IS THE S-S BOND FOR FOLDING AND STABILITY?

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU A 1001

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

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site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU B 1001

Chain	Residue
B	MET251
B	GLY175
B	HIS176
B	CYS242
B	HIS247

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site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU C 1001

Chain	Residue
C	GLY305
C	HIS306
C	CYS372
C	HIS377
C	MET381

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site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CU D 1001

Chain	Residue
D	GLY435
D	HIS436
D	CYS502
D	PHE504
D	HIS507
D	MET511

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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

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269|PubMed:1420141

Chain	Residue	Details
A	HIS46
D	HIS436
D	CYS502
D	HIS507
A	CYS112
A	HIS117
B	HIS176
B	CYS242
B	HIS247
C	HIS306
C	CYS372
C	HIS377

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site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING:

Chain	Residue	Details
A	MET121
B	MET251
C	MET381
D	MET511

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