2BBK

CRYSTAL STRUCTURE OF THE QUINOPROTEIN METHYLAMINE DEHYDROGENASE FROM PARACOCCUS DENITRIFICANS AT 1.75 ANGSTROMS

Functional Information from GO Data

Chain	GOid	namespace	contents
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
J	0016491	molecular_function	oxidoreductase activity
J	0030058	molecular_function	aliphatic amine dehydrogenase activity
J	0030416	biological_process	methylamine metabolic process
J	0042597	cellular_component	periplasmic space
J	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
M	0009308	biological_process	amine metabolic process
M	0016491	molecular_function	oxidoreductase activity
M	0016638	molecular_function	oxidoreductase activity, acting on the CH-NH2 group of donors
M	0030288	cellular_component	outer membrane-bounded periplasmic space
M	0042597	cellular_component	periplasmic space
M	0052876	molecular_function	methylamine dehydrogenase (amicyanin) activity

Functional Information from PDB Data

site_id	TQL
Number of Residues	2
Details

Chain	Residue
L	TRQ57
L	TRP108

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site_id	TQM
Number of Residues	2
Details

Chain	Residue
M	TRQ57
M	TRP108

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	MOD_RES: Tryptophylquinone => ECO:0000269|PubMed:1409575

Chain	Residue	Details
L	TRQ57
M	TRQ57

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site_id	SWS_FT_FI2
Number of Residues	4
Details	CROSSLNK: Tryptophan tryptophylquinone (Trp-Trp) => ECO:0000269|PubMed:1409575

Chain	Residue	Details
L	TRQ57
L	TRP108
M	TRQ57
M	TRP108

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	6
Details	a catalytic site defined by CSA, PubMed 1599920, 8140419, 9514722, Singh2000

Chain	Residue	Details
L	ASP76
L	THR122
L	ASP32
L	TYR119
L	TRQ57
L	TRP108

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site_id	CSA2
Number of Residues	5
Details	a catalytic site defined by CSA, PubMed 1599920, 8140419, 9514722, Singh2000

Chain	Residue	Details
M	ASP76
M	THR122
M	ASP32
M	TYR119
M	TRP108

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site_id	MCSA1
Number of Residues	6
Details	M-CSA 13

Chain	Residue	Details
L	ASP32	electrostatic stabiliser, proton acceptor, proton donor
L	TRQ57	proton acceptor, proton donor, proton relay
L	ASP76	electrostatic stabiliser, proton acceptor, proton donor
L	TRP108	proton acceptor, proton donor, proton relay, single electron donor
L	TYR119	steric role
L	THR122	electrostatic stabiliser

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site_id	MCSA2
Number of Residues	6
Details	M-CSA 13

Chain	Residue	Details
M	ASP32	electrostatic stabiliser, proton acceptor, proton donor
M	TRQ57	proton acceptor, proton donor, proton relay
M	ASP76	electrostatic stabiliser, proton acceptor, proton donor
M	TRP108	proton acceptor, proton donor, proton relay, single electron donor
M	TYR119	steric role
M	THR122	electrostatic stabiliser

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