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2J57

X-ray reduced Paraccocus denitrificans methylamine dehydrogenase N- quinol 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
C0005507molecular_functioncopper ion binding
C0009055molecular_functionelectron transfer activity
C0042597cellular_componentperiplasmic space
C0046872molecular_functionmetal ion binding
D0005507molecular_functioncopper ion binding
D0009055molecular_functionelectron transfer activity
D0042597cellular_componentperiplasmic space
D0046872molecular_functionmetal ion binding
G0016491molecular_functionoxidoreductase activity
G0030058molecular_functionaliphatic amine dehydrogenase activity
G0030416biological_processmethylamine metabolic process
G0042597cellular_componentperiplasmic space
G0052876molecular_functionmethylamine dehydrogenase (amicyanin) activity
H0016491molecular_functionoxidoreductase activity
H0030058molecular_functionaliphatic amine dehydrogenase activity
H0030416biological_processmethylamine metabolic process
H0042597cellular_componentperiplasmic space
H0052876molecular_functionmethylamine dehydrogenase (amicyanin) activity
I0016491molecular_functionoxidoreductase activity
I0030058molecular_functionaliphatic amine dehydrogenase activity
I0030416biological_processmethylamine metabolic process
I0042597cellular_componentperiplasmic space
I0052876molecular_functionmethylamine dehydrogenase (amicyanin) activity
J0016491molecular_functionoxidoreductase activity
J0030058molecular_functionaliphatic amine dehydrogenase activity
J0030416biological_processmethylamine metabolic process
J0042597cellular_componentperiplasmic space
J0052876molecular_functionmethylamine dehydrogenase (amicyanin) activity
K0009308biological_processamine metabolic process
K0016491molecular_functionoxidoreductase activity
K0016638molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors
K0030288cellular_componentouter membrane-bounded periplasmic space
K0042597cellular_componentperiplasmic space
K0052876molecular_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
N0009308biological_processamine metabolic process
N0016491molecular_functionoxidoreductase activity
N0016638molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors
N0030288cellular_componentouter membrane-bounded periplasmic space
N0042597cellular_componentperiplasmic space
N0052876molecular_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 Residues4
DetailsBINDING SITE FOR RESIDUE CU C 1106
ChainResidue
CCYS92
CHIS95
CMET98
CHIS53

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU D 1106
ChainResidue
DHIS53
DCYS92
DHIS95
DMET98

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 Residues4
DetailsMOD_RES: Tryptophylquinone => ECO:0000269|PubMed:1409575
ChainResidueDetails
KTQQ57
CCYS92
CHIS95
CMET98
DHIS53
DCYS92
DHIS95
DMET98
LTQQ57
MTQQ57
NTQQ57
BHIS53
BCYS92
BHIS95
BMET98
CHIS53

site_idSWS_FT_FI2
Number of Residues8
DetailsCROSSLNK: Tryptophan tryptophylquinone (Trp-Trp) => ECO:0000269|PubMed:1409575
ChainResidueDetails
KTQQ57
KTRP108
LTQQ57
LTRP108
MTQQ57
MTRP108
NTQQ57
NTRP108

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 2bbk
ChainResidueDetails
KASP76
KTHR122
KASP32
KTYR119
KTRP108

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 2bbk
ChainResidueDetails
LASP76
LTHR122
LASP32
LTYR119
LTRP108

site_idCSA3
Number of Residues5
DetailsAnnotated By Reference To The Literature 2bbk
ChainResidueDetails
MASP76
MTHR122
MASP32
MTYR119
MTRP108

site_idCSA4
Number of Residues5
DetailsAnnotated By Reference To The Literature 2bbk
ChainResidueDetails
NASP76
NTHR122
NASP32
NTYR119
NTRP108

site_idMCSA1
Number of Residues6
DetailsM-CSA 13
ChainResidueDetails
IASP32electrostatic stabiliser, proton acceptor, proton donor
IALA57proton acceptor, proton donor, proton relay
ILEU80electrostatic stabiliser, proton acceptor, proton donor
IGLU112proton acceptor, proton donor, proton relay, single electron donor
IALA123steric role
IGLU126electrostatic stabiliser

site_idMCSA2
Number of Residues6
DetailsM-CSA 13
ChainResidueDetails
JASP32electrostatic stabiliser, proton acceptor, proton donor
JALA57proton acceptor, proton donor, proton relay
JLEU80electrostatic stabiliser, proton acceptor, proton donor
JGLU112proton acceptor, proton donor, proton relay, single electron donor
JALA123steric role
JGLU126electrostatic stabiliser

site_idMCSA3
Number of Residues6
DetailsM-CSA 13
ChainResidueDetails
KASP32electrostatic stabiliser, proton acceptor, proton donor
KTQQ57proton acceptor, proton donor, proton relay
KTYR80electrostatic stabiliser, proton acceptor, proton donor
KALA112proton acceptor, proton donor, proton relay, single electron donor
KILE123steric role
KILE126electrostatic stabiliser

site_idMCSA4
Number of Residues6
DetailsM-CSA 13
ChainResidueDetails
LASP32electrostatic stabiliser, proton acceptor, proton donor
LTQQ57proton acceptor, proton donor, proton relay
LTYR80electrostatic stabiliser, proton acceptor, proton donor
LALA112proton acceptor, proton donor, proton relay, single electron donor
LILE123steric role
LILE126electrostatic stabiliser

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PDB entries from 2025-07-02

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