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2J55

X-ray reduced Paraccocus denitrificans methylamine dehydrogenase O- quinone in complex with amicyanin.

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0009055molecular_functionelectron transfer activity
A0042597cellular_componentperiplasmic space
A0046872molecular_functionmetal ion binding
B0005507molecular_functioncopper ion binding
B0009055molecular_functionelectron transfer activity
B0042597cellular_componentperiplasmic space
B0046872molecular_functionmetal ion binding
H0016491molecular_functionoxidoreductase activity
H0030058molecular_functionaliphatic amine dehydrogenase activity
H0030416biological_processmethylamine metabolic process
H0042597cellular_componentperiplasmic space
H0052876molecular_functionmethylamine dehydrogenase (amicyanin) activity
J0016491molecular_functionoxidoreductase activity
J0030058molecular_functionaliphatic amine dehydrogenase activity
J0030416biological_processmethylamine metabolic process
J0042597cellular_componentperiplasmic space
J0052876molecular_functionmethylamine dehydrogenase (amicyanin) activity
L0009308biological_processamine metabolic process
L0016491molecular_functionoxidoreductase activity
L0016638molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors
L0030288cellular_componentouter membrane-bounded periplasmic space
L0042597cellular_componentperiplasmic space
L0052876molecular_functionmethylamine dehydrogenase (amicyanin) activity
M0009308biological_processamine metabolic process
M0016491molecular_functionoxidoreductase activity
M0016638molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors
M0030288cellular_componentouter membrane-bounded periplasmic space
M0042597cellular_componentperiplasmic space
M0052876molecular_functionmethylamine dehydrogenase (amicyanin) activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU A 1106
ChainResidue
AHIS53
ACYS92
AHIS95
AMET98

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU B 1106
ChainResidue
BHIS53
BCYS92
BHIS95
BMET98

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL H 1387
ChainResidue
HHIS250
HLEU262
HALA264
HHOH2277
HPHE220

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL H 1388
ChainResidue
HHIS54
HTRP282
HGLN378
HHOH2392
HHOH2402
LHOH2021

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL H 1389
ChainResidue
HGLN14
HALA18
HARG70
HHOH2012
HHOH2403
HHOH2405
HHOH2406
MASP37

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL L 1132
ChainResidue
HARG305
LCYS23
LCYS88
LLEU89
LASN90
LHOH2048
LHOH2073
LHOH2074
LHOH2075

Functional Information from PROSITE/UniProt
site_idPS00196
Number of Residues14
DetailsCOPPER_BLUE Type-1 copper (blue) proteins signature. AgtYdYHCt.P.Hpf..M
ChainResidueDetails
AALA85-MET98

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues208
DetailsDomain: {"description":"Plastocyanin-like"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"Tryptophylquinone","evidences":[{"source":"PubMed","id":"1409575","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 2bbk
ChainResidueDetails
LASP76
LTHR122
LASP32
LTYR119
LTRP108

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 2bbk
ChainResidueDetails
MASP76
MTHR122
MASP32
MTYR119
MTRP108

site_idMCSA1
Number of Residues6
DetailsM-CSA 13
ChainResidueDetails

site_idMCSA2
Number of Residues6
DetailsM-CSA 13
ChainResidueDetails

238895

PDB entries from 2025-07-16

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