1MG3
MUTATION OF ALPHA PHE55 OF METHYLAMINE DEHYDROGENASE ALTERS THE REORGANIZATION ENERGY AND ELECTRONIC COUPLING FOR ITS ELECTRON TRANSFER REACTION WITH AMICYANIN
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0030058 | molecular_function | amine dehydrogenase activity |
A | 0030416 | biological_process | methylamine metabolic process |
A | 0042597 | cellular_component | periplasmic space |
B | 0009308 | biological_process | amine metabolic process |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016638 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors |
B | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
B | 0042597 | cellular_component | periplasmic space |
B | 0052876 | molecular_function | methylamine dehydrogenase (amicyanin) activity |
C | 0005507 | molecular_function | copper ion binding |
C | 0009055 | molecular_function | electron transfer activity |
C | 0042597 | cellular_component | periplasmic space |
C | 0046872 | molecular_function | metal ion binding |
D | 0005506 | molecular_function | iron ion binding |
D | 0009055 | molecular_function | electron transfer activity |
D | 0015945 | biological_process | methanol metabolic process |
D | 0020037 | molecular_function | heme binding |
D | 0042597 | cellular_component | periplasmic space |
D | 0046872 | molecular_function | metal ion binding |
E | 0030058 | molecular_function | amine dehydrogenase activity |
E | 0030416 | biological_process | methylamine metabolic process |
E | 0042597 | cellular_component | periplasmic space |
F | 0009308 | biological_process | amine metabolic process |
F | 0016491 | molecular_function | oxidoreductase activity |
F | 0016638 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors |
F | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
F | 0042597 | cellular_component | periplasmic space |
F | 0052876 | molecular_function | methylamine dehydrogenase (amicyanin) activity |
G | 0005507 | molecular_function | copper ion binding |
G | 0009055 | molecular_function | electron transfer activity |
G | 0042597 | cellular_component | periplasmic space |
G | 0046872 | molecular_function | metal ion binding |
H | 0005506 | molecular_function | iron ion binding |
H | 0009055 | molecular_function | electron transfer activity |
H | 0015945 | biological_process | methanol metabolic process |
H | 0020037 | molecular_function | heme binding |
H | 0042597 | cellular_component | periplasmic space |
H | 0046872 | molecular_function | metal ion binding |
I | 0030058 | molecular_function | amine dehydrogenase activity |
I | 0030416 | biological_process | methylamine metabolic process |
I | 0042597 | cellular_component | periplasmic space |
J | 0009308 | biological_process | amine metabolic process |
J | 0016491 | molecular_function | oxidoreductase activity |
J | 0016638 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors |
J | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
J | 0042597 | cellular_component | periplasmic space |
J | 0052876 | molecular_function | methylamine dehydrogenase (amicyanin) activity |
K | 0005507 | molecular_function | copper ion binding |
K | 0009055 | molecular_function | electron transfer activity |
K | 0042597 | cellular_component | periplasmic space |
K | 0046872 | molecular_function | metal ion binding |
L | 0005506 | molecular_function | iron ion binding |
L | 0009055 | molecular_function | electron transfer activity |
L | 0015945 | biological_process | methanol metabolic process |
L | 0020037 | molecular_function | heme binding |
L | 0042597 | cellular_component | periplasmic space |
L | 0046872 | molecular_function | metal ion binding |
M | 0030058 | molecular_function | amine dehydrogenase activity |
M | 0030416 | biological_process | methylamine metabolic process |
M | 0042597 | cellular_component | periplasmic space |
N | 0009308 | biological_process | amine metabolic process |
N | 0016491 | molecular_function | oxidoreductase activity |
N | 0016638 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors |
N | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
N | 0042597 | cellular_component | periplasmic space |
N | 0052876 | molecular_function | methylamine dehydrogenase (amicyanin) activity |
O | 0005507 | molecular_function | copper ion binding |
O | 0009055 | molecular_function | electron transfer activity |
O | 0042597 | cellular_component | periplasmic space |
O | 0046872 | molecular_function | metal ion binding |
P | 0005506 | molecular_function | iron ion binding |
P | 0009055 | molecular_function | electron transfer activity |
P | 0015945 | biological_process | methanol metabolic process |
P | 0020037 | molecular_function | heme binding |
P | 0042597 | cellular_component | periplasmic space |
P | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CU C 107 |
Chain | Residue |
C | HIS53 |
C | CYS92 |
C | HIS95 |
C | MET98 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CU G 107 |
Chain | Residue |
G | HIS53 |
G | CYS92 |
G | HIS95 |
G | MET98 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CU K 107 |
Chain | Residue |
K | CYS92 |
K | HIS95 |
K | MET98 |
K | HIS53 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CU O 107 |
Chain | Residue |
O | HIS53 |
O | CYS92 |
O | HIS95 |
O | MET98 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 F 401 |
Chain | Residue |
F | PHE110 |
F | GLY111 |
F | ASP115 |
F | HOH1550 |
G | LYS68 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 B 402 |
Chain | Residue |
B | PHE110 |
B | GLY111 |
B | ASP115 |
B | HOH1222 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 J 403 |
Chain | Residue |
J | PHE110 |
J | GLY111 |
J | ASP115 |
J | HOH1305 |
K | LYS68 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 O 404 |
Chain | Residue |
N | PHE110 |
N | GLY111 |
N | ASP115 |
O | LYS68 |
O | HOH1725 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 I 405 |
Chain | Residue |
I | ALA86 |
I | ASP87 |
I | ASP88 |
I | PRO146 |
I | ASP147 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PO4 E 406 |
Chain | Residue |
E | ALA86 |
E | ASP87 |
E | ASP88 |
E | PRO146 |
E | GLY148 |
E | HOH1178 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 M 407 |
Chain | Residue |
M | ALA86 |
M | ASP87 |
M | ASP88 |
M | PRO146 |
M | HOH1280 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PO4 A 408 |
Chain | Residue |
A | ALA86 |
A | ASP87 |
A | ASP88 |
A | PRO146 |
A | ASP147 |
A | GLY148 |
site_id | BC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA P 601 |
Chain | Residue |
O | GLU31 |
P | GLY72 |
P | ASP75 |
P | TYR77 |
P | HOH1132 |
P | HOH1289 |
site_id | BC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA L 602 |
Chain | Residue |
K | GLU31 |
L | GLY72 |
L | ASP75 |
L | TYR77 |
L | HOH1155 |
site_id | BC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA D 603 |
Chain | Residue |
C | GLU31 |
D | GLY72 |
D | ASP75 |
D | TYR77 |
D | HOH1177 |
site_id | BC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NA H 604 |
Chain | Residue |
G | GLU31 |
H | GLY72 |
H | ASP75 |
H | TYR77 |
site_id | BC8 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE HEC D 200 |
Chain | Residue |
D | MET56 |
D | CYS57 |
D | CYS60 |
D | HIS61 |
D | TRP78 |
D | THR79 |
D | TYR80 |
D | ASN83 |
D | LEU93 |
D | THR98 |
D | GLN100 |
D | MET101 |
site_id | BC9 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE HEC H 200 |
Chain | Residue |
H | THR92 |
H | LEU93 |
H | ALA97 |
H | THR98 |
H | GLN100 |
H | MET101 |
H | MET104 |
H | MET56 |
H | CYS57 |
H | CYS60 |
H | HIS61 |
H | PRO71 |
H | TRP78 |
H | THR79 |
H | TYR80 |
H | ASN83 |
H | LEU89 |
site_id | CC1 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE HEC L 200 |
Chain | Residue |
L | MET56 |
L | CYS57 |
L | CYS60 |
L | HIS61 |
L | PRO71 |
L | TRP78 |
L | THR79 |
L | TYR80 |
L | ASN83 |
L | LEU89 |
L | THR92 |
L | LEU93 |
L | THR98 |
L | GLN100 |
L | MET101 |
site_id | CC2 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE HEC P 200 |
Chain | Residue |
P | MET56 |
P | CYS57 |
P | CYS60 |
P | HIS61 |
P | PRO71 |
P | TRP78 |
P | THR79 |
P | TYR80 |
P | ASN83 |
P | LEU89 |
P | THR92 |
P | LEU93 |
P | ALA97 |
P | THR98 |
P | GLN100 |
P | MET101 |
P | HOH1189 |
Functional Information from PROSITE/UniProt
site_id | PS00196 |
Number of Residues | 14 |
Details | COPPER_BLUE Type-1 copper (blue) proteins signature. AgtYdYHCt.P.Hpf..M |
Chain | Residue | Details |
C | ALA85-MET98 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | BINDING: covalent |
Chain | Residue | Details |
D | CYS57 | |
K | CYS92 | |
K | HIS95 | |
K | MET98 | |
O | HIS53 | |
O | CYS92 | |
O | HIS95 | |
O | MET98 | |
D | CYS60 | |
H | CYS57 | |
H | CYS60 | |
L | CYS57 | |
L | CYS60 | |
P | CYS57 | |
P | CYS60 | |
K | HIS53 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: axial binding residue |
Chain | Residue | Details |
D | HIS61 | |
H | HIS61 | |
L | HIS61 | |
P | HIS61 | |
J | TRW57 | |
J | TRP108 | |
N | TRW57 | |
N | TRP108 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 2bbk |
Chain | Residue | Details |
B | ASP76 | |
B | THR122 | |
B | ASP32 | |
B | TYR119 | |
B | TRP108 |
site_id | CSA2 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 2bbk |
Chain | Residue | Details |
F | ASP76 | |
F | THR122 | |
F | ASP32 | |
F | TYR119 | |
F | TRP108 |
site_id | CSA3 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 2bbk |
Chain | Residue | Details |
J | ASP76 | |
J | THR122 | |
J | ASP32 | |
J | TYR119 | |
J | TRP108 |
site_id | CSA4 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 2bbk |
Chain | Residue | Details |
N | ASP76 | |
N | THR122 | |
N | ASP32 | |
N | TYR119 | |
N | TRP108 |
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 13 |
Chain | Residue | Details |
B | ASP32 | electrostatic stabiliser, proton acceptor, proton donor |
B | TRW57 | proton acceptor, proton donor, proton relay |
B | ASP76 | electrostatic stabiliser, proton acceptor, proton donor |
B | TRP108 | proton acceptor, proton donor, proton relay, single electron donor |
B | TYR119 | steric role |
B | THR122 | electrostatic stabiliser |
site_id | MCSA2 |
Number of Residues | 6 |
Details | M-CSA 13 |
Chain | Residue | Details |
F | ASP32 | electrostatic stabiliser, proton acceptor, proton donor |
F | TRW57 | proton acceptor, proton donor, proton relay |
F | ASP76 | electrostatic stabiliser, proton acceptor, proton donor |
F | TRP108 | proton acceptor, proton donor, proton relay, single electron donor |
F | TYR119 | steric role |
F | THR122 | electrostatic stabiliser |
site_id | MCSA3 |
Number of Residues | 6 |
Details | M-CSA 13 |
Chain | Residue | Details |
J | ASP32 | electrostatic stabiliser, proton acceptor, proton donor |
J | TRW57 | proton acceptor, proton donor, proton relay |
J | ASP76 | electrostatic stabiliser, proton acceptor, proton donor |
J | TRP108 | proton acceptor, proton donor, proton relay, single electron donor |
J | TYR119 | steric role |
J | THR122 | electrostatic stabiliser |
site_id | MCSA4 |
Number of Residues | 6 |
Details | M-CSA 13 |
Chain | Residue | Details |
N | ASP32 | electrostatic stabiliser, proton acceptor, proton donor |
N | TRW57 | proton acceptor, proton donor, proton relay |
N | ASP76 | electrostatic stabiliser, proton acceptor, proton donor |
N | TRP108 | proton acceptor, proton donor, proton relay, single electron donor |
N | TYR119 | steric role |
N | THR122 | electrostatic stabiliser |