2IAA

Crystal Structure of an Electron Transfer Complex Between Aromatic Amine Dephydrogenase and Azurin from Alcaligenes Faecalis (Form 2)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0030058	molecular_function	amine dehydrogenase activity
A	0042597	cellular_component	periplasmic space
B	0009308	biological_process	amine metabolic process
B	0016491	molecular_function	oxidoreductase activity
B	0016638	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors
B	0030059	molecular_function	aralkylamine dehydrogenase (azurin) activity
B	0042597	cellular_component	periplasmic space
C	0005507	molecular_function	copper ion binding
C	0009055	molecular_function	electron transfer activity
C	0042597	cellular_component	periplasmic space
C	0046872	molecular_function	metal ion binding
D	0030058	molecular_function	amine dehydrogenase activity
D	0042597	cellular_component	periplasmic space
E	0009308	biological_process	amine metabolic process
E	0016491	molecular_function	oxidoreductase activity
E	0016638	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors
E	0030059	molecular_function	aralkylamine dehydrogenase (azurin) activity
E	0042597	cellular_component	periplasmic space

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU C 130

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

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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. GedYaFFCsfPgHwsi.M

Chain	Residue	Details
C	GLY105-MET121

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:17087503

Chain	Residue	Details
C	HIS46
C	CYS112
C	HIS117
C	MET121
D	LEU57
D	ASN81

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site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000269|PubMed:16614214, ECO:0000269|PubMed:17005560

Chain	Residue	Details
B	ASP81
E	ASP81

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site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:16614214, ECO:0000269|PubMed:17005560

Chain	Residue	Details
B	ASP37
B	ASN109
E	ASP37
E	ASN109

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site_id	SWS_FT_FI4
Number of Residues	2
Details	SITE: Transition state stabilizer

Chain	Residue	Details
B	THR125
E	THR125

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site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Tryptophylquinone => ECO:0000269|PubMed:16614214, ECO:0000269|PubMed:17005560, ECO:0000269|PubMed:17087503

Chain	Residue	Details
B	TRQ62
E	TRQ62

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site_id	SWS_FT_FI6
Number of Residues	4
Details	CROSSLNK: Tryptophan tryptophylquinone (Trp-Trp) => ECO:0000269|PubMed:16614214, ECO:0000269|PubMed:17005560, ECO:0000269|PubMed:17087503

Chain	Residue	Details
B	TRQ62
B	TRP113
E	TRQ62
E	TRP113

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	5
Details	Annotated By Reference To The Literature 2bbk

Chain	Residue	Details
B	ASP81
B	TRP113
B	PHE122
B	ASP37
B	THR125

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site_id	CSA2
Number of Residues	5
Details	Annotated By Reference To The Literature 2bbk

Chain	Residue	Details
E	ASP81
E	TRP113
E	PHE122
E	ASP37
E	THR125

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