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2J56

X-ray reduced Paraccocus denitrificans methylamine dehydrogenase N- semiquinone 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 NA L 1132
ChainResidue
LTQQ57
LASN104
LILE106
LHOH2055
LASP32

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA M 1131
ChainResidue
MASP32
MTQQ57
MASN104
MILE106
MHOH2072

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL H 1387
ChainResidue
HILE228
HASN229
HHIS230
HTRP282
HGLN284
HLYS307
HHOH2417
LASP105

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 Residues2
DetailsMOD_RES: Tryptophylquinone => ECO:0000269|PubMed:1409575
ChainResidueDetails
LTQQ57
MTQQ57
AHIS95
AMET98
BHIS53
BCYS92
BHIS95
BMET98

site_idSWS_FT_FI2
Number of Residues4
DetailsCROSSLNK: Tryptophan tryptophylquinone (Trp-Trp) => ECO:0000269|PubMed:1409575
ChainResidueDetails
LTQQ57
LTRP108
MTQQ57
MTRP108

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

237735

PDB entries from 2025-06-18

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