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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_functionamine dehydrogenase activity
H0030416biological_processmethylamine metabolic process
H0042597cellular_componentperiplasmic space
H0052876molecular_functionmethylamine dehydrogenase (amicyanin) activity
J0016491molecular_functionoxidoreductase activity
J0030058molecular_functionamine 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 Residues2
DetailsMOD_RES: Tryptophylquinone => ECO:0000269|PubMed:1409575
ChainResidueDetails
LTRQ57
MTRQ57
AHIS95
AMET98
BHIS53
BCYS92
BHIS95
BMET98

site_idSWS_FT_FI2
Number of Residues4
DetailsCROSSLNK: Tryptophan tryptophylquinone (Trp-Trp) => ECO:0000269|PubMed:1409575
ChainResidueDetails
LTRQ57
LTRP108
MTRQ57
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
LASP32electrostatic stabiliser, proton acceptor, proton donor
LTRQ57proton acceptor, proton donor, proton relay
LASP76electrostatic stabiliser, proton acceptor, proton donor
LTRP108proton acceptor, proton donor, proton relay, single electron donor
LTYR119steric role
LTHR122electrostatic stabiliser

site_idMCSA2
Number of Residues6
DetailsM-CSA 13
ChainResidueDetails
MASP32electrostatic stabiliser, proton acceptor, proton donor
MTRQ57proton acceptor, proton donor, proton relay
MASP76electrostatic stabiliser, proton acceptor, proton donor
MTRP108proton acceptor, proton donor, proton relay, single electron donor
MTYR119steric role
MTHR122electrostatic stabiliser

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PDB entries from 2024-07-17

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