Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2GC4

Structural comparison of the oxidized ternary electron transfer complex of methylamine dehydrogenase, amicyanin and cytochrome c551i from Paracoccus denitrificans with the substrate-reduced, copper free complex at 1.9 A resolution.

Functional Information from GO Data
ChainGOidnamespacecontents
A0016491molecular_functionoxidoreductase activity
A0030058molecular_functionamine dehydrogenase activity
A0030416biological_processmethylamine metabolic process
A0042597cellular_componentperiplasmic space
A0052876molecular_functionmethylamine dehydrogenase (amicyanin) activity
B0009308biological_processamine metabolic process
B0016491molecular_functionoxidoreductase activity
B0016638molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors
B0030288cellular_componentouter membrane-bounded periplasmic space
B0042597cellular_componentperiplasmic space
B0052876molecular_functionmethylamine dehydrogenase (amicyanin) activity
C0005507molecular_functioncopper ion binding
C0009055molecular_functionelectron transfer activity
C0042597cellular_componentperiplasmic space
C0046872molecular_functionmetal ion binding
D0005506molecular_functioniron ion binding
D0009055molecular_functionelectron transfer activity
D0015945biological_processmethanol metabolic process
D0020037molecular_functionheme binding
D0042597cellular_componentperiplasmic space
D0046872molecular_functionmetal ion binding
E0016491molecular_functionoxidoreductase activity
E0030058molecular_functionamine dehydrogenase activity
E0030416biological_processmethylamine metabolic process
E0042597cellular_componentperiplasmic space
E0052876molecular_functionmethylamine dehydrogenase (amicyanin) activity
F0009308biological_processamine metabolic process
F0016491molecular_functionoxidoreductase activity
F0016638molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors
F0030288cellular_componentouter membrane-bounded periplasmic space
F0042597cellular_componentperiplasmic space
F0052876molecular_functionmethylamine dehydrogenase (amicyanin) activity
G0005507molecular_functioncopper ion binding
G0009055molecular_functionelectron transfer activity
G0042597cellular_componentperiplasmic space
G0046872molecular_functionmetal ion binding
H0005506molecular_functioniron ion binding
H0009055molecular_functionelectron transfer activity
H0015945biological_processmethanol metabolic process
H0020037molecular_functionheme binding
H0042597cellular_componentperiplasmic space
H0046872molecular_functionmetal ion binding
I0016491molecular_functionoxidoreductase activity
I0030058molecular_functionamine dehydrogenase activity
I0030416biological_processmethylamine metabolic process
I0042597cellular_componentperiplasmic space
I0052876molecular_functionmethylamine dehydrogenase (amicyanin) activity
J0009308biological_processamine metabolic process
J0016491molecular_functionoxidoreductase activity
J0016638molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors
J0030288cellular_componentouter membrane-bounded periplasmic space
J0042597cellular_componentperiplasmic space
J0052876molecular_functionmethylamine dehydrogenase (amicyanin) activity
K0005507molecular_functioncopper ion binding
K0009055molecular_functionelectron transfer activity
K0042597cellular_componentperiplasmic space
K0046872molecular_functionmetal ion binding
L0005506molecular_functioniron ion binding
L0009055molecular_functionelectron transfer activity
L0015945biological_processmethanol metabolic process
L0020037molecular_functionheme binding
L0042597cellular_componentperiplasmic space
L0046872molecular_functionmetal ion binding
M0016491molecular_functionoxidoreductase activity
M0030058molecular_functionamine dehydrogenase activity
M0030416biological_processmethylamine metabolic process
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
O0005507molecular_functioncopper ion binding
O0009055molecular_functionelectron transfer activity
O0042597cellular_componentperiplasmic space
O0046872molecular_functionmetal ion binding
P0005506molecular_functioniron ion binding
P0009055molecular_functionelectron transfer activity
P0015945biological_processmethanol metabolic process
P0020037molecular_functionheme binding
P0042597cellular_componentperiplasmic space
P0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU G 107
ChainResidue
GHIS53
GCYS92
GHIS95
GMET98

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU K 107
ChainResidue
KHIS53
KCYS92
KHIS95
KMET98

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU O 107
ChainResidue
OCYS92
OHIS95
OMET98
OHIS53

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU C 107
ChainResidue
CHIS53
CCYS92
CHIS95
CMET98

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA L 601
ChainResidue
KGLU31
LGLY72
LASP75
LTYR77
LHOH1056
LHOH1513

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NA P 602
ChainResidue
OGLU31
PGLY72
PASP75
PTYR77
PHOH1246
PHOH1495
PHOH2138

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NA H 603
ChainResidue
GGLU31
HGLY72
HASP75
HTYR77
HHOH1083
HHOH1553
HHOH1763

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NA D 604
ChainResidue
CHOH2139
DGLY72
DASP75
DTYR77
DHOH1001
DHOH2053
DHOH2140

site_idAC9
Number of Residues17
DetailsBINDING SITE FOR RESIDUE HEC H 200
ChainResidue
HMET56
HCYS57
HCYS60
HHIS61
HPRO71
HLEU73
HTRP78
HTHR79
HTYR80
HASN83
HLEU89
HLEU93
HALA97
HTHR98
HGLN100
HMET101
HHOH1763

site_idBC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE HEC L 200
ChainResidue
LMET56
LCYS57
LCYS60
LHIS61
LPRO71
LLEU73
LTRP78
LTHR79
LTYR80
LASN83
LLEU89
LALA97
LTHR98
LGLN100
LMET101
LHOH1513

site_idBC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE HEC D 200
ChainResidue
DMET56
DCYS57
DCYS60
DHIS61
DPRO71
DLEU73
DTRP78
DTHR79
DTYR80
DASN83
DLEU89
DLEU93
DALA97
DTHR98
DGLN100
DMET101
DHOH2053

site_idBC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE HEC P 200
ChainResidue
PTRP78
PTHR79
PTYR80
PASN83
PLEU93
PALA97
PTHR98
PGLN100
PMET101
PHOH2138
PMET56
PCYS57
PCYS60
PHIS61
PPRO71
PLEU73

Functional Information from PROSITE/UniProt
site_idPS00196
Number of Residues14
DetailsCOPPER_BLUE Type-1 copper (blue) proteins signature. AgtYdYHCt.P.Hpf..M
ChainResidueDetails
CALA85-MET98

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: covalent
ChainResidueDetails
DCYS57
KCYS92
KHIS95
KMET98
OHIS53
OCYS92
OHIS95
OMET98
DCYS60
HCYS57
HCYS60
LCYS57
LCYS60
PCYS57
PCYS60
KHIS53

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: axial binding residue
ChainResidueDetails
DHIS61
HHIS61
LHIS61
PHIS61
JTRQ57
JTRP108
NTRQ57
NTRP108

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 13
ChainResidueDetails
BASP32electrostatic stabiliser, proton acceptor, proton donor
BTRQ57proton acceptor, proton donor, proton relay
BASP76electrostatic stabiliser, proton acceptor, proton donor
BTRP108proton acceptor, proton donor, proton relay, single electron donor
BTYR119steric role
BTHR122electrostatic stabiliser

site_idMCSA2
Number of Residues6
DetailsM-CSA 13
ChainResidueDetails
FASP32electrostatic stabiliser, proton acceptor, proton donor
FTRQ57proton acceptor, proton donor, proton relay
FASP76electrostatic stabiliser, proton acceptor, proton donor
FTRP108proton acceptor, proton donor, proton relay, single electron donor
FTYR119steric role
FTHR122electrostatic stabiliser

site_idMCSA3
Number of Residues6
DetailsM-CSA 13
ChainResidueDetails
JASP32electrostatic stabiliser, proton acceptor, proton donor
JTRQ57proton acceptor, proton donor, proton relay
JASP76electrostatic stabiliser, proton acceptor, proton donor
JTRP108proton acceptor, proton donor, proton relay, single electron donor
JTYR119steric role
JTHR122electrostatic stabiliser

site_idMCSA4
Number of Residues6
DetailsM-CSA 13
ChainResidueDetails
NASP32electrostatic stabiliser, proton acceptor, proton donor
NTRQ57proton acceptor, proton donor, proton relay
NASP76electrostatic stabiliser, proton acceptor, proton donor
NTRP108proton acceptor, proton donor, proton relay, single electron donor
NTYR119steric role
NTHR122electrostatic stabiliser

217705

PDB entries from 2024-03-27

PDB statisticsPDBj update infoContact PDBjnumon