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	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU A 0

Chain	Residue
A	CYS92
A	HIS95
A	MET98
A	HIS53

---

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 H 0

Chain	Residue
H	LYS341
H	HIS362
H	HIS362

---

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

Chain	Residue
C	MET56
C	CYS57
C	CYS60
C	HIS61
C	PRO71
C	TRP78
C	THR79
C	TYR80
C	ASN83
C	LEU89
C	THR92
C	LEU93
C	ALA97
C	THR98
C	GLN100
C	MET101
C	MET104

---

site_id	COP
Number of Residues	5
Details

Chain	Residue
A	CU0
H	GLY53
H	GLY92
H	THR95
H	VAL98

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site_id	HEM
Number of Residues	1
Details

Chain	Residue
C	HEC200

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site_id	TTQ
Number of Residues	2
Details

Chain	Residue
H	ARG57
H	PRO108

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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

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Modified residue: {"description":"Tryptophylquinone","evidences":[{"source":"PubMed","id":"1409575","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	104
Details	Domain: {"description":"Plastocyanin-like"}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"description":"covalent"}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	1
Details	Binding site: {"description":"axial binding residue"}

Chain

Residue

Details

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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
L	ASP76
L	THR122
L	ASP32
L	TYR119
L	TRP108

---

site_id	MCSA1
Number of Residues	6
Details	M-CSA 13

Chain	Residue	Details
A	ALA66	steric role

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