2MTA

CRYSTAL STRUCTURE OF A TERNARY ELECTRON TRANSFER COMPLEX BETWEEN METHYLAMINE DEHYDROGENASE, AMICYANIN AND A C-TYPE CYTOCHROME

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005507	molecular_function	copper ion binding
A	0009055	molecular_function	electron transfer activity
A	0042597	cellular_component	periplasmic space
A	0046872	molecular_function	metal ion binding
C	0005506	molecular_function	iron ion binding
C	0009055	molecular_function	electron transfer activity
C	0015945	biological_process	methanol metabolic process
C	0020037	molecular_function	heme binding
C	0042597	cellular_component	periplasmic space
C	0046872	molecular_function	metal ion binding
H	0016491	molecular_function	oxidoreductase activity
H	0030058	molecular_function	aliphatic amine dehydrogenase activity
H	0030416	biological_process	methylamine metabolic process
H	0042597	cellular_component	periplasmic space
H	0052876	molecular_function	methylamine dehydrogenase (amicyanin) activity
L	0009308	biological_process	amine metabolic process
L	0016491	molecular_function	oxidoreductase activity
L	0016638	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors
L	0030288	cellular_component	outer membrane-bounded periplasmic space
L	0042597	cellular_component	periplasmic space
L	0052876	molecular_function	methylamine dehydrogenase (amicyanin) activity

Functional Information from PDB Data

site_id	AC3
Number of Residues	17
Details	BINDING SITE FOR RESIDUE HEC C 200

Chain	Residue
C	HEC200

Functional Information from PROSITE/UniProt

site_id	PS00196
Number of Residues	14
Details	COPPER_BLUE Type-1 copper (blue) proteins signature. AgtYdYHCt.P.Hpf..M

Chain	Residue	Details
A	ALA85-MET98

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: axial binding residue

Catalytic Information from CSA

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

Chain	Residue	Details
A	ALA66	steric role