3PCH
STRUCTURE OF PROTOCATECHUATE 3,4-DIOXYGENASE COMPLEXED WITH 3-CHLORO-4-HYDROXYBENZOATE
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0005506 | molecular_function | iron ion binding |
A | 0008199 | molecular_function | ferric iron binding |
A | 0009056 | biological_process | catabolic process |
A | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
A | 0018578 | molecular_function | protocatechuate 3,4-dioxygenase activity |
A | 0042952 | biological_process | beta-ketoadipate pathway |
A | 0051213 | molecular_function | dioxygenase activity |
B | 0003824 | molecular_function | catalytic activity |
B | 0005506 | molecular_function | iron ion binding |
B | 0008199 | molecular_function | ferric iron binding |
B | 0009056 | biological_process | catabolic process |
B | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
B | 0018578 | molecular_function | protocatechuate 3,4-dioxygenase activity |
B | 0042952 | biological_process | beta-ketoadipate pathway |
B | 0051213 | molecular_function | dioxygenase activity |
C | 0003824 | molecular_function | catalytic activity |
C | 0005506 | molecular_function | iron ion binding |
C | 0008199 | molecular_function | ferric iron binding |
C | 0009056 | biological_process | catabolic process |
C | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
C | 0018578 | molecular_function | protocatechuate 3,4-dioxygenase activity |
C | 0042952 | biological_process | beta-ketoadipate pathway |
C | 0051213 | molecular_function | dioxygenase activity |
D | 0003824 | molecular_function | catalytic activity |
D | 0005506 | molecular_function | iron ion binding |
D | 0008199 | molecular_function | ferric iron binding |
D | 0009056 | biological_process | catabolic process |
D | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
D | 0018578 | molecular_function | protocatechuate 3,4-dioxygenase activity |
D | 0042952 | biological_process | beta-ketoadipate pathway |
D | 0051213 | molecular_function | dioxygenase activity |
E | 0003824 | molecular_function | catalytic activity |
E | 0005506 | molecular_function | iron ion binding |
E | 0008199 | molecular_function | ferric iron binding |
E | 0009056 | biological_process | catabolic process |
E | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
E | 0018578 | molecular_function | protocatechuate 3,4-dioxygenase activity |
E | 0042952 | biological_process | beta-ketoadipate pathway |
E | 0051213 | molecular_function | dioxygenase activity |
F | 0003824 | molecular_function | catalytic activity |
F | 0005506 | molecular_function | iron ion binding |
F | 0008199 | molecular_function | ferric iron binding |
F | 0009056 | biological_process | catabolic process |
F | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
F | 0018578 | molecular_function | protocatechuate 3,4-dioxygenase activity |
F | 0042952 | biological_process | beta-ketoadipate pathway |
F | 0051213 | molecular_function | dioxygenase activity |
M | 0003824 | molecular_function | catalytic activity |
M | 0005506 | molecular_function | iron ion binding |
M | 0008199 | molecular_function | ferric iron binding |
M | 0009056 | biological_process | catabolic process |
M | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
M | 0018578 | molecular_function | protocatechuate 3,4-dioxygenase activity |
M | 0019619 | biological_process | 3,4-dihydroxybenzoate catabolic process |
M | 0042952 | biological_process | beta-ketoadipate pathway |
M | 0046872 | molecular_function | metal ion binding |
M | 0051213 | molecular_function | dioxygenase activity |
N | 0003824 | molecular_function | catalytic activity |
N | 0005506 | molecular_function | iron ion binding |
N | 0008199 | molecular_function | ferric iron binding |
N | 0009056 | biological_process | catabolic process |
N | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
N | 0018578 | molecular_function | protocatechuate 3,4-dioxygenase activity |
N | 0019619 | biological_process | 3,4-dihydroxybenzoate catabolic process |
N | 0042952 | biological_process | beta-ketoadipate pathway |
N | 0046872 | molecular_function | metal ion binding |
N | 0051213 | molecular_function | dioxygenase activity |
O | 0003824 | molecular_function | catalytic activity |
O | 0005506 | molecular_function | iron ion binding |
O | 0008199 | molecular_function | ferric iron binding |
O | 0009056 | biological_process | catabolic process |
O | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
O | 0018578 | molecular_function | protocatechuate 3,4-dioxygenase activity |
O | 0019619 | biological_process | 3,4-dihydroxybenzoate catabolic process |
O | 0042952 | biological_process | beta-ketoadipate pathway |
O | 0046872 | molecular_function | metal ion binding |
O | 0051213 | molecular_function | dioxygenase activity |
P | 0003824 | molecular_function | catalytic activity |
P | 0005506 | molecular_function | iron ion binding |
P | 0008199 | molecular_function | ferric iron binding |
P | 0009056 | biological_process | catabolic process |
P | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
P | 0018578 | molecular_function | protocatechuate 3,4-dioxygenase activity |
P | 0019619 | biological_process | 3,4-dihydroxybenzoate catabolic process |
P | 0042952 | biological_process | beta-ketoadipate pathway |
P | 0046872 | molecular_function | metal ion binding |
P | 0051213 | molecular_function | dioxygenase activity |
Q | 0003824 | molecular_function | catalytic activity |
Q | 0005506 | molecular_function | iron ion binding |
Q | 0008199 | molecular_function | ferric iron binding |
Q | 0009056 | biological_process | catabolic process |
Q | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
Q | 0018578 | molecular_function | protocatechuate 3,4-dioxygenase activity |
Q | 0019619 | biological_process | 3,4-dihydroxybenzoate catabolic process |
Q | 0042952 | biological_process | beta-ketoadipate pathway |
Q | 0046872 | molecular_function | metal ion binding |
Q | 0051213 | molecular_function | dioxygenase activity |
R | 0003824 | molecular_function | catalytic activity |
R | 0005506 | molecular_function | iron ion binding |
R | 0008199 | molecular_function | ferric iron binding |
R | 0009056 | biological_process | catabolic process |
R | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
R | 0018578 | molecular_function | protocatechuate 3,4-dioxygenase activity |
R | 0019619 | biological_process | 3,4-dihydroxybenzoate catabolic process |
R | 0042952 | biological_process | beta-ketoadipate pathway |
R | 0046872 | molecular_function | metal ion binding |
R | 0051213 | molecular_function | dioxygenase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FE M 600 |
Chain | Residue |
M | TYR408 |
M | TYR447 |
M | HIS460 |
M | HIS462 |
M | CHB550 |
M | HOH742 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FE N 600 |
Chain | Residue |
N | TYR408 |
N | TYR447 |
N | HIS460 |
N | HIS462 |
N | CHB550 |
N | HOH846 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FE O 600 |
Chain | Residue |
O | TYR408 |
O | TYR447 |
O | HIS460 |
O | HIS462 |
O | CHB550 |
O | HOH861 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FE P 600 |
Chain | Residue |
P | TYR408 |
P | TYR447 |
P | HIS460 |
P | HIS462 |
P | CHB550 |
P | HOH778 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FE Q 600 |
Chain | Residue |
Q | TYR408 |
Q | TYR447 |
Q | HIS460 |
Q | HIS462 |
Q | CHB550 |
Q | HOH774 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FE R 600 |
Chain | Residue |
R | TYR408 |
R | TYR447 |
R | HIS460 |
R | HIS462 |
R | CHB550 |
R | HOH861 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE BME M 601 |
Chain | Residue |
M | HIS361 |
M | CYS429 |
M | SER438 |
M | HOH691 |
site_id | AC8 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE CHB M 550 |
Chain | Residue |
A | THR12 |
A | GLY14 |
A | PRO15 |
A | ARG133 |
M | TYR324 |
M | TYR447 |
M | TRP449 |
M | ARG457 |
M | HIS460 |
M | HIS462 |
M | GLN477 |
M | ILE491 |
M | FE600 |
M | HOH742 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CHB M 551 |
Chain | Residue |
M | ARG333 |
M | HOH680 |
M | HOH736 |
M | HOH746 |
O | ILE328 |
site_id | ACA |
Number of Residues | 28 |
Details | SITE "ACA" IS THE ACTIVE SITE OF THE PROTOMER CONSISTING OF CHAINS A AND M. |
Chain | Residue |
A | THR12 |
M | TRP400 |
M | TYR408 |
M | TYR447 |
M | PRO448 |
M | TRP449 |
M | ARG450 |
M | ARG457 |
M | HIS460 |
M | HIS462 |
M | GLN477 |
A | ALA13 |
M | ILE491 |
M | CHB550 |
M | FE600 |
M | HOH605 |
A | HOH606 |
M | HOH625 |
M | HOH633 |
M | HOH634 |
M | HOH742 |
A | GLY14 |
A | PRO15 |
A | TYR16 |
A | ARG133 |
A | GLY134 |
M | TYR324 |
M | THR326 |
site_id | ACB |
Number of Residues | 28 |
Details | SITE "ACB" IS THE ACTIVE SITE OF THE PROTOMER CONSISTING OF CHAINS B AND N. |
Chain | Residue |
B | THR12 |
B | ALA13 |
B | GLY14 |
B | PRO15 |
B | TYR16 |
B | ARG133 |
B | GLY134 |
N | TYR324 |
N | THR326 |
N | TRP400 |
N | TYR408 |
N | TYR447 |
N | PRO448 |
N | TRP449 |
N | ARG450 |
N | ARG457 |
N | HIS460 |
N | HIS462 |
N | GLN477 |
N | ILE491 |
N | CHB550 |
N | FE600 |
N | HOH699 |
B | HOH606 |
N | HOH721 |
N | HOH729 |
N | HOH730 |
N | HOH846 |
site_id | ACC |
Number of Residues | 28 |
Details | SITE "ACC" IS THE ACTIVE SITE OF THE PROTOMER CONSISTING OF CHAINS C AND O. |
Chain | Residue |
C | THR12 |
C | ALA13 |
C | GLY14 |
C | PRO15 |
C | TYR16 |
C | ARG133 |
C | GLY134 |
O | TYR324 |
O | THR326 |
O | TRP400 |
O | TYR408 |
O | TYR447 |
O | PRO448 |
O | TRP449 |
O | ARG450 |
O | ARG457 |
O | HIS460 |
O | HIS462 |
O | GLN477 |
O | ILE491 |
O | CHB550 |
O | FE600 |
O | HOH605 |
C | HOH606 |
O | HOH643 |
O | HOH659 |
O | HOH660 |
O | HOH861 |
site_id | ACD |
Number of Residues | 28 |
Details | SITE "ACD" IS THE ACTIVE SITE OF THE PROTOMER CONSISTING OF CHAINS D AND P. |
Chain | Residue |
P | ARG457 |
P | HIS460 |
P | HIS462 |
P | GLN477 |
P | ILE491 |
P | CHB550 |
P | FE600 |
D | HOH605 |
D | HOH606 |
P | HOH666 |
P | HOH674 |
P | HOH675 |
P | HOH778 |
D | THR12 |
D | ALA13 |
D | GLY14 |
D | PRO15 |
D | TYR16 |
D | ARG133 |
D | GLY134 |
P | TYR324 |
P | THR326 |
P | TRP400 |
P | TYR408 |
P | TYR447 |
P | PRO448 |
P | TRP449 |
P | ARG450 |
site_id | ACE |
Number of Residues | 28 |
Details | SITE "ACE" IS THE ACTIVE SITE OF THE PROTOMER CONSISTING OF CHAINS E AND Q. |
Chain | Residue |
E | THR12 |
E | ALA13 |
E | GLY14 |
E | PRO15 |
E | TYR16 |
E | ARG133 |
E | GLY134 |
Q | TYR324 |
Q | THR326 |
Q | TRP400 |
Q | TYR408 |
Q | TYR447 |
Q | PRO448 |
Q | TRP449 |
Q | ARG450 |
Q | ARG457 |
Q | HIS460 |
Q | HIS462 |
Q | GLN477 |
Q | ILE491 |
Q | CHB550 |
Q | FE600 |
Q | HOH626 |
E | HOH606 |
Q | HOH651 |
Q | HOH659 |
Q | HOH660 |
Q | HOH774 |
site_id | ACF |
Number of Residues | 28 |
Details | SITE "ACF" IS THE ACTIVE SITE OF THE PROTOMER CONSISTING OF CHAINS F AND R. |
Chain | Residue |
F | THR12 |
F | ALA13 |
F | GLY14 |
F | PRO15 |
F | TYR16 |
F | ARG133 |
F | GLY134 |
R | TYR324 |
R | THR326 |
R | TRP400 |
R | TYR408 |
R | TYR447 |
R | PRO448 |
R | TRP449 |
R | ARG450 |
R | ARG457 |
R | HIS460 |
R | HIS462 |
R | GLN477 |
R | ILE491 |
R | CHB550 |
R | FE600 |
R | HOH605 |
F | HOH606 |
R | HOH643 |
R | HOH659 |
R | HOH660 |
R | HOH861 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE BME N 601 |
Chain | Residue |
N | HIS361 |
N | CYS429 |
N | LEU430 |
N | SER438 |
site_id | BC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE CHB N 550 |
Chain | Residue |
B | THR12 |
B | PRO15 |
B | ARG133 |
N | TYR324 |
N | TYR408 |
N | TYR447 |
N | TRP449 |
N | ARG457 |
N | HIS460 |
N | HIS462 |
N | GLN477 |
N | ILE491 |
N | FE600 |
N | HOH846 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CHB N 551 |
Chain | Residue |
M | PRO322 |
M | ILE328 |
M | HOH749 |
N | ARG333 |
N | HOH777 |
N | HOH840 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE BME O 601 |
Chain | Residue |
O | HIS361 |
O | CYS429 |
O | SER438 |
O | HOH751 |
site_id | BC5 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE CHB O 550 |
Chain | Residue |
C | THR12 |
C | PRO15 |
C | ARG133 |
O | TYR324 |
O | TYR408 |
O | TYR447 |
O | TRP449 |
O | ARG457 |
O | HIS460 |
O | HIS462 |
O | GLN477 |
O | ILE491 |
O | FE600 |
O | HOH861 |
site_id | BC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CHB O 551 |
Chain | Residue |
N | PRO322 |
N | ILE328 |
O | ARG333 |
O | HOH732 |
O | HOH847 |
O | HOH868 |
site_id | BC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE BME P 601 |
Chain | Residue |
P | HIS361 |
P | CYS429 |
P | LEU430 |
P | SER438 |
P | HOH730 |
site_id | BC8 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE CHB P 550 |
Chain | Residue |
D | THR12 |
D | GLY14 |
D | PRO15 |
D | ARG133 |
P | TYR324 |
P | TYR447 |
P | TRP449 |
P | ARG457 |
P | HIS460 |
P | HIS462 |
P | GLN477 |
P | ILE491 |
P | FE600 |
P | HOH778 |
site_id | BC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CHB P 551 |
Chain | Residue |
P | ARG333 |
P | HOH719 |
P | HOH772 |
P | HOH781 |
R | PRO322 |
R | ILE328 |
site_id | CC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE BME Q 601 |
Chain | Residue |
Q | HIS361 |
Q | CYS429 |
Q | LEU430 |
Q | SER438 |
Q | HOH719 |
site_id | CC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE CHB Q 550 |
Chain | Residue |
E | THR12 |
E | GLY14 |
E | PRO15 |
Q | TYR324 |
Q | TYR408 |
Q | TYR447 |
Q | TRP449 |
Q | ARG457 |
Q | HIS460 |
Q | HIS462 |
Q | GLN477 |
Q | ILE491 |
Q | FE600 |
Q | HOH774 |
site_id | CC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CHB Q 551 |
Chain | Residue |
P | ILE328 |
Q | ARG333 |
Q | HOH708 |
Q | HOH768 |
Q | HOH779 |
site_id | CC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE BME R 601 |
Chain | Residue |
R | HIS361 |
R | CYS429 |
R | LEU430 |
R | SER438 |
R | HOH751 |
site_id | CC5 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE CHB R 550 |
Chain | Residue |
F | THR12 |
F | PRO15 |
F | ARG133 |
R | TYR324 |
R | TYR408 |
R | TYR447 |
R | TRP449 |
R | ARG457 |
R | HIS460 |
R | HIS462 |
R | GLN477 |
R | ILE491 |
R | FE600 |
R | HOH861 |
site_id | CC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CHB R 551 |
Chain | Residue |
Q | PRO322 |
Q | ILE328 |
R | ARG333 |
R | HOH732 |
R | HOH847 |
R | HOH868 |
site_id | S2M |
Number of Residues | 45 |
Details | SECONDARY THREE-FOLD SITE BETWEEN M, N, O CHAINS. |
Chain | Residue |
M | LYS318 |
M | LEU320 |
M | PRO322 |
M | ILE328 |
M | PRO332 |
M | ARG333 |
M | GLN334 |
M | CHB551 |
M | HOH680 |
M | HOH697 |
M | HOH709 |
O | HOH846 |
M | HOH736 |
M | HOH744 |
M | HOH746 |
N | LYS318 |
N | LEU320 |
N | PRO322 |
N | ILE328 |
N | PRO332 |
N | ARG333 |
N | GLN334 |
N | CHB551 |
N | HOH777 |
N | HOH795 |
N | HOH808 |
M | HOH748 |
N | HOH840 |
N | HOH849 |
M | HOH749 |
O | LYS318 |
O | LEU320 |
O | PRO322 |
O | ILE328 |
O | PRO332 |
O | ARG333 |
O | GLN334 |
O | CHB551 |
O | HOH732 |
O | HOH760 |
O | HOH784 |
N | HOH853 |
O | HOH847 |
O | HOH865 |
O | HOH868 |
site_id | S2P |
Number of Residues | 45 |
Details | SECONDARY THREE-FOLD SITE BETWEEN P, Q, R CHAINS. |
Chain | Residue |
P | LYS318 |
P | LEU320 |
P | PRO322 |
P | ILE328 |
P | PRO332 |
P | ARG333 |
P | GLN334 |
P | CHB551 |
P | HOH719 |
P | HOH736 |
P | HOH747 |
R | HOH846 |
P | HOH772 |
P | HOH779 |
P | HOH781 |
Q | LYS318 |
Q | LEU320 |
Q | PRO322 |
Q | ILE328 |
Q | PRO332 |
Q | ARG333 |
Q | GLN334 |
Q | CHB551 |
Q | HOH708 |
Q | HOH725 |
Q | HOH737 |
P | HOH783 |
Q | HOH768 |
Q | HOH777 |
Q | HOH779 |
R | LYS318 |
R | LEU320 |
R | PRO322 |
R | ILE328 |
R | PRO332 |
R | ARG333 |
R | GLN334 |
R | CHB551 |
R | HOH732 |
R | HOH760 |
R | HOH784 |
Q | HOH781 |
R | HOH847 |
R | HOH865 |
R | HOH868 |
site_id | VEA |
Number of Residues | 29 |
Details | SITE "VEA" IS THE VESTIGIAL SITE OF THE PROTOMER CONSISTING OF CHAINS A AND M. |
Chain | Residue |
A | TYR79 |
A | VAL114 |
A | ASN115 |
A | ASN116 |
A | ALA117 |
A | ALA118 |
A | MET122 |
A | HIS125 |
A | ASN127 |
A | ARG142 |
A | VAL157 |
M | ASP304 |
M | ARG307 |
M | ILE339 |
M | PRO340 |
M | GLN341 |
M | SER342 |
M | ILE343 |
M | SER344 |
M | GLU345 |
A | HOH646 |
M | HOH631 |
M | HOH638 |
A | HOH673 |
M | HOH644 |
A | HOH683 |
M | HOH660 |
A | HOH725 |
N | HOH696 |
site_id | VEB |
Number of Residues | 29 |
Details | SITE "VEB" IS THE VESTIGIAL SITE OF THE PROTOMER CONSISTING OF CHAINS B AND N. |
Chain | Residue |
B | TYR79 |
B | VAL114 |
B | ASN115 |
B | ASN116 |
B | ALA117 |
B | ALA118 |
B | MET122 |
B | HIS125 |
B | ASN127 |
B | ARG142 |
B | VAL157 |
N | ASP304 |
N | ARG307 |
N | ILE339 |
N | PRO340 |
N | GLN341 |
N | SER342 |
N | ILE343 |
N | SER344 |
N | GLU345 |
B | HOH646 |
N | HOH727 |
N | HOH734 |
B | HOH673 |
N | HOH741 |
N | HOH743 |
N | HOH757 |
N | HOH771 |
O | HOH795 |
site_id | VEC |
Number of Residues | 29 |
Details | SITE "VEC" IS THE VESTIGIAL SITE OF THE PROTOMER CONSISTING OF CHAINS C AND O. |
Chain | Residue |
C | TYR79 |
C | VAL114 |
C | ASN115 |
C | ASN116 |
C | ALA117 |
C | ALA118 |
C | MET122 |
C | HIS125 |
C | ASN127 |
C | ARG142 |
C | VAL157 |
O | ASP304 |
O | ARG307 |
O | ILE339 |
O | PRO340 |
O | GLN341 |
O | SER342 |
O | ILE343 |
O | SER344 |
O | GLU345 |
C | HOH646 |
O | HOH655 |
O | HOH666 |
C | HOH673 |
O | HOH681 |
C | HOH683 |
O | HOH707 |
C | HOH725 |
M | HOH752 |
site_id | VED |
Number of Residues | 29 |
Details | SITE "VED" IS THE VESTIGIAL SITE OF THE PROTOMER CONSISTING OF CHAINS D AND P. |
Chain | Residue |
D | TYR79 |
D | VAL114 |
D | ASN115 |
D | ASN116 |
D | ALA117 |
D | ALA118 |
D | MET122 |
D | HIS125 |
D | ASN127 |
D | ARG142 |
D | VAL157 |
P | ASP304 |
P | ARG307 |
P | ILE339 |
P | PRO340 |
P | GLN341 |
P | SER342 |
P | ILE343 |
P | SER344 |
P | GLU345 |
D | HOH646 |
P | HOH672 |
D | HOH666 |
D | HOH673 |
P | HOH685 |
D | HOH683 |
P | HOH700 |
D | HOH725 |
Q | HOH624 |
site_id | VEE |
Number of Residues | 29 |
Details | SITE "VEE" IS THE VESTIGIAL SITE OF THE PROTOMER CONSISTING OF CHAINS E AND Q. |
Chain | Residue |
E | TYR79 |
E | VAL114 |
E | ASN115 |
E | ASN116 |
E | ALA117 |
E | ALA118 |
E | MET122 |
E | HIS125 |
E | ASN127 |
E | ARG142 |
E | VAL157 |
Q | ASP304 |
Q | ARG307 |
Q | ILE339 |
Q | PRO340 |
Q | GLN341 |
Q | SER342 |
Q | ILE343 |
Q | SER344 |
Q | GLU345 |
E | HOH646 |
E | HOH655 |
E | HOH666 |
E | HOH673 |
Q | HOH672 |
E | HOH683 |
Q | HOH687 |
E | HOH725 |
R | HOH795 |
site_id | VEF |
Number of Residues | 29 |
Details | SITE "VEF" IS THE VESTIGIAL SITE OF THE PROTOMER CONSISTING OF CHAINS F AND R. |
Chain | Residue |
F | TYR79 |
F | VAL114 |
F | ASN115 |
F | ASN116 |
F | ALA117 |
F | ALA118 |
F | MET122 |
F | HIS125 |
F | ASN127 |
F | ARG142 |
F | VAL157 |
R | ASP304 |
R | ARG307 |
R | ILE339 |
R | PRO340 |
R | GLN341 |
R | SER342 |
R | ILE343 |
R | SER344 |
R | GLU345 |
F | HOH646 |
R | HOH655 |
R | HOH666 |
F | HOH673 |
R | HOH681 |
R | HOH683 |
R | HOH707 |
R | HOH725 |
P | HOH786 |
Functional Information from PROSITE/UniProt
site_id | PS00083 |
Number of Residues | 29 |
Details | INTRADIOL_DIOXYGENAS Intradiol ring-cleavage dioxygenases signature. VaGrVvdqyGkpVpntlVEMwqanagGrY |
Chain | Residue | Details |
M | VAL380-TYR408 | |
A | LEU51-TYR79 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000269|PubMed:7990141 |
Chain | Residue | Details |
M | ARG409 | |
O | PRO448 | |
O | ILE461 | |
O | PHE463 | |
P | ARG409 | |
P | PRO448 | |
P | ILE461 | |
P | PHE463 | |
Q | ARG409 | |
Q | PRO448 | |
Q | ILE461 | |
M | PRO448 | |
Q | PHE463 | |
R | ARG409 | |
R | PRO448 | |
R | ILE461 | |
R | PHE463 | |
M | ILE461 | |
M | PHE463 | |
N | ARG409 | |
N | PRO448 | |
N | ILE461 | |
N | PHE463 | |
O | ARG409 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 3pca |
Chain | Residue | Details |
M | TYR447 | |
M | ARG457 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 3pca |
Chain | Residue | Details |
N | TYR447 | |
N | ARG457 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 3pca |
Chain | Residue | Details |
O | TYR447 | |
O | ARG457 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 3pca |
Chain | Residue | Details |
P | TYR447 | |
P | ARG457 |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 3pca |
Chain | Residue | Details |
Q | TYR447 | |
Q | ARG457 |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 3pca |
Chain | Residue | Details |
R | TYR447 | |
R | ARG457 |
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 936 |
Chain | Residue | Details |
M | ARG409 | metal ligand |
M | PRO448 | metal ligand, proton shuttle (general acid/base) |
M | PRO458 | electrostatic stabiliser |
M | ILE461 | metal ligand |
M | PHE463 | metal ligand |
site_id | MCSA2 |
Number of Residues | 5 |
Details | M-CSA 936 |
Chain | Residue | Details |
N | ARG409 | metal ligand |
N | PRO448 | metal ligand, proton shuttle (general acid/base) |
N | PRO458 | electrostatic stabiliser |
N | ILE461 | metal ligand |
N | PHE463 | metal ligand |
site_id | MCSA3 |
Number of Residues | 5 |
Details | M-CSA 936 |
Chain | Residue | Details |
O | ARG409 | metal ligand |
O | PRO448 | metal ligand, proton shuttle (general acid/base) |
O | PRO458 | electrostatic stabiliser |
O | ILE461 | metal ligand |
O | PHE463 | metal ligand |
site_id | MCSA4 |
Number of Residues | 5 |
Details | M-CSA 936 |
Chain | Residue | Details |
P | ARG409 | metal ligand |
P | PRO448 | metal ligand, proton shuttle (general acid/base) |
P | PRO458 | electrostatic stabiliser |
P | ILE461 | metal ligand |
P | PHE463 | metal ligand |
site_id | MCSA5 |
Number of Residues | 5 |
Details | M-CSA 936 |
Chain | Residue | Details |
Q | ARG409 | metal ligand |
Q | PRO448 | metal ligand, proton shuttle (general acid/base) |
Q | PRO458 | electrostatic stabiliser |
Q | ILE461 | metal ligand |
Q | PHE463 | metal ligand |
site_id | MCSA6 |
Number of Residues | 5 |
Details | M-CSA 936 |
Chain | Residue | Details |
R | ARG409 | metal ligand |
R | PRO448 | metal ligand, proton shuttle (general acid/base) |
R | PRO458 | electrostatic stabiliser |
R | ILE461 | metal ligand |
R | PHE463 | metal ligand |