3LKT
Tyrosine 447 of Protocatechuate 3,4-Dioxygenase Controls Efficient Progress Through Catalysis
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 | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 201 |
Chain | Residue |
A | ASN37 |
A | THR105 |
A | HIS107 |
A | HOH1777 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE BME A 202 |
Chain | Residue |
A | GLY191 |
A | GLU192 |
A | HOH2075 |
A | TYR56 |
A | ASP57 |
A | ARG188 |
A | ILE189 |
A | GLN190 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE TRS A 203 |
Chain | Residue |
A | THR169 |
A | ILE171 |
A | ARG184 |
A | PHE185 |
A | ASP186 |
A | ARG188 |
A | HOH2346 |
A | HOH2672 |
A | HOH2673 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FE M 600 |
Chain | Residue |
M | BME29 |
M | TYR408 |
M | HIS460 |
M | HIS462 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CL M 7 |
Chain | Residue |
M | LYS325 |
M | ILE328 |
M | ALA329 |
M | HOH2298 |
M | HOH2546 |
O | HOH38 |
site_id | AC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL M 8 |
Chain | Residue |
M | HIS534 |
M | PHE535 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL M 9 |
Chain | Residue |
M | CYS429 |
M | LEU430 |
M | HOH931 |
site_id | AC8 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL M 14 |
Chain | Residue |
M | ARG383 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL M 16 |
Chain | Residue |
M | GLN503 |
M | ILE505 |
M | LYS507 |
M | ARG522 |
M | PHE523 |
M | ASP524 |
site_id | BC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE BME M 21 |
Chain | Residue |
A | PRO15 |
A | ARG133 |
M | BME29 |
M | TYR324 |
M | THR326 |
M | TRP449 |
M | ILE491 |
M | HOH874 |
M | HOH2281 |
M | HOH2282 |
M | HOH2291 |
site_id | BC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE BME M 29 |
Chain | Residue |
A | PRO15 |
A | TYR16 |
M | BME21 |
M | HOH225 |
M | TYR408 |
M | ARG457 |
M | HIS460 |
M | HIS462 |
M | FE600 |
site_id | BC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE BME M 36 |
Chain | Residue |
M | ILE339 |
M | PRO340 |
M | HOH1268 |
M | HOH2624 |
M | HOH2651 |
N | ARG450 |
N | PRO453 |
Q | PRO515 |
site_id | BC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE BME M 47 |
Chain | Residue |
M | ARG409 |
M | PRO421 |
site_id | BC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 201 |
Chain | Residue |
B | ASN37 |
B | THR105 |
B | HIS107 |
site_id | BC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE TRS B 202 |
Chain | Residue |
B | GLU168 |
B | THR169 |
B | ILE171 |
B | ARG184 |
B | PHE185 |
B | ASP186 |
B | ARG188 |
B | HOH2480 |
B | HOH2620 |
site_id | BC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FE N 600 |
Chain | Residue |
N | BME32 |
N | TYR408 |
N | HIS460 |
N | HIS462 |
site_id | BC8 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL N 13 |
Chain | Residue |
N | ARG383 |
site_id | BC9 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE BME N 18 |
Chain | Residue |
B | PRO15 |
B | ARG133 |
N | TYR324 |
N | THR326 |
N | TRP449 |
N | ILE491 |
N | HOH542 |
N | HOH2277 |
N | HOH2292 |
site_id | CC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE BME N 32 |
Chain | Residue |
B | PRO15 |
B | TYR16 |
N | TYR408 |
N | ARG457 |
N | HIS460 |
N | HIS462 |
N | HOH552 |
N | FE600 |
N | HOH2285 |
site_id | CC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE BME N 37 |
Chain | Residue |
N | PHE535 |
site_id | CC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE BME N 44 |
Chain | Residue |
N | GLN503 |
N | PHE523 |
N | ASP524 |
N | HOH2609 |
site_id | CC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 C 201 |
Chain | Residue |
C | ASN37 |
C | ARG38 |
C | THR105 |
C | HIS107 |
site_id | CC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL C 202 |
Chain | Residue |
C | GLU168 |
C | ILE171 |
C | ARG184 |
C | PHE185 |
C | ASP186 |
C | ARG188 |
C | HOH223 |
site_id | CC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE BME C 203 |
Chain | Residue |
C | TYR56 |
C | ASP57 |
C | ARG188 |
C | ILE189 |
C | GLN190 |
C | GLY191 |
C | GLU192 |
site_id | CC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FE O 600 |
Chain | Residue |
O | BME30 |
O | TYR408 |
O | HIS460 |
O | HIS462 |
site_id | CC8 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL O 12 |
Chain | Residue |
O | ARG383 |
site_id | CC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE BME O 27 |
Chain | Residue |
O | PHE535 |
O | HOH1701 |
site_id | DC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE BME O 30 |
Chain | Residue |
C | PRO15 |
C | TYR16 |
O | TYR408 |
O | ARG457 |
O | HIS460 |
O | HIS462 |
O | FE600 |
O | HOH605 |
site_id | DC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE BME O 33 |
Chain | Residue |
C | PRO15 |
C | ARG133 |
O | HOH253 |
O | TYR324 |
O | THR326 |
O | TRP449 |
O | ILE491 |
O | HOH2279 |
O | HOH2280 |
site_id | DC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE BME O 42 |
Chain | Residue |
O | HOH44 |
O | THR321 |
O | PRO322 |
O | ASP323 |
O | HOH559 |
O | HOH1820 |
site_id | DC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE BME O 45 |
Chain | Residue |
O | ARG522 |
O | PHE523 |
O | ASP524 |
O | HOH2610 |
site_id | DC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE BME O 49 |
Chain | Residue |
D | GLU176 |
O | PHE356 |
O | CYS429 |
O | LEU430 |
O | HOH1460 |
O | HOH2487 |
site_id | DC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 D 201 |
Chain | Residue |
D | ASN37 |
D | THR105 |
D | HIS107 |
D | HOH1092 |
D | HOH1436 |
site_id | DC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE TRS D 202 |
Chain | Residue |
D | THR169 |
D | ILE171 |
D | ARG184 |
D | PHE185 |
D | ASP186 |
D | ARG188 |
D | HOH2590 |
site_id | DC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FE P 600 |
Chain | Residue |
P | BME31 |
P | TYR408 |
P | HIS460 |
P | HIS462 |
site_id | DC9 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL P 15 |
Chain | Residue |
P | ARG383 |
site_id | EC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE BME P 22 |
Chain | Residue |
D | GLY14 |
D | PRO15 |
D | ARG133 |
P | TYR324 |
P | THR326 |
P | TRP449 |
P | ILE491 |
P | HOH811 |
P | HOH2286 |
P | HOH2287 |
P | HOH2650 |
site_id | EC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE BME P 23 |
Chain | Residue |
P | GLN503 |
P | ILE505 |
P | PHE523 |
P | ASP524 |
P | HOH2294 |
P | HOH2393 |
site_id | EC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE BME P 25 |
Chain | Residue |
P | PHE356 |
P | CYS429 |
P | LEU430 |
P | HOH1204 |
site_id | EC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE BME P 31 |
Chain | Residue |
D | PRO15 |
D | TYR16 |
P | TYR408 |
P | ARG457 |
P | HIS460 |
P | HIS462 |
P | HOH540 |
P | FE600 |
site_id | EC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE BME P 35 |
Chain | Residue |
P | ARG407 |
P | PRO418 |
P | LEU419 |
site_id | EC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE BME P 40 |
Chain | Residue |
P | HOH21 |
P | ASN454 |
P | ASP455 |
P | MET488 |
R | HOH678 |
site_id | EC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE BME P 41 |
Chain | Residue |
P | THR533 |
P | PHE535 |
site_id | EC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE BME P 48 |
Chain | Residue |
P | ARG409 |
P | PRO421 |
site_id | EC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 E 201 |
Chain | Residue |
E | ASN37 |
E | THR105 |
E | HIS107 |
site_id | FC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE TRS E 202 |
Chain | Residue |
E | GLU168 |
E | THR169 |
E | ILE171 |
E | ALA172 |
E | ARG184 |
E | PHE185 |
E | ASP186 |
E | ARG188 |
E | HOH2517 |
E | HOH2621 |
site_id | FC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FE Q 600 |
Chain | Residue |
Q | BME34 |
Q | TYR408 |
Q | HIS460 |
Q | HIS462 |
site_id | FC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL Q 11 |
Chain | Residue |
Q | ARG383 |
site_id | FC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE BME Q 19 |
Chain | Residue |
E | PRO15 |
E | ARG133 |
Q | TYR324 |
Q | THR326 |
Q | TRP449 |
Q | ILE491 |
Q | HOH626 |
Q | HOH2278 |
Q | HOH2452 |
site_id | FC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE BME Q 24 |
Chain | Residue |
Q | GLN503 |
Q | PHE523 |
Q | ASP524 |
Q | HOH2332 |
site_id | FC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE BME Q 34 |
Chain | Residue |
E | PRO15 |
E | TYR16 |
Q | HOH251 |
Q | TYR408 |
Q | ARG457 |
Q | HIS460 |
Q | HIS462 |
Q | FE600 |
Q | HOH623 |
site_id | FC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE BME Q 46 |
Chain | Residue |
Q | PHE356 |
Q | CYS429 |
Q | LEU430 |
Q | HOH1300 |
site_id | FC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 F 201 |
Chain | Residue |
F | ASN37 |
F | ARG38 |
F | THR105 |
F | HIS107 |
site_id | FC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE TRS F 202 |
Chain | Residue |
F | THR169 |
F | ILE171 |
F | ARG184 |
F | PHE185 |
F | ASP186 |
F | ARG188 |
F | HOH2665 |
site_id | GC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FE R 600 |
Chain | Residue |
R | BME28 |
R | TYR408 |
R | HIS460 |
R | HIS462 |
site_id | GC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL R 10 |
Chain | Residue |
R | ARG383 |
site_id | GC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE BME R 20 |
Chain | Residue |
F | PRO15 |
F | ARG133 |
R | HOH188 |
R | TYR324 |
R | THR326 |
R | TRP449 |
R | HOH2289 |
R | HOH2290 |
site_id | GC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE BME R 26 |
Chain | Residue |
R | HIS534 |
R | PHE535 |
R | HOH1839 |
site_id | GC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE BME R 28 |
Chain | Residue |
F | PRO15 |
F | TYR16 |
R | HOH35 |
R | TYR408 |
R | ARG457 |
R | HIS460 |
R | HIS462 |
R | FE600 |
site_id | GC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE BME R 43 |
Chain | Residue |
B | ILE2 |
R | ARG522 |
R | PHE523 |
R | ASP524 |
R | HOH2611 |
Functional Information from PROSITE/UniProt
site_id | PS00083 |
Number of Residues | 29 |
Details | INTRADIOL_DIOXYGENAS Intradiol ring-cleavage dioxygenases signature. LlGqVydgnGhlVrdsfLEVwqadanGeY |
Chain | Residue | Details |
A | LEU51-TYR79 | |
M | VAL380-TYR408 |
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 | TYR408 | |
O | HIS447 | |
O | HIS460 | |
O | HIS462 | |
P | TYR408 | |
P | HIS447 | |
P | HIS460 | |
P | HIS462 | |
Q | TYR408 | |
Q | HIS447 | |
Q | HIS460 | |
M | HIS447 | |
Q | HIS462 | |
R | TYR408 | |
R | HIS447 | |
R | HIS460 | |
R | HIS462 | |
M | HIS460 | |
M | HIS462 | |
N | TYR408 | |
N | HIS447 | |
N | HIS460 | |
N | HIS462 | |
O | TYR408 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 936 |
Chain | Residue | Details |
M | TYR408 | metal ligand |
M | HIS447 | metal ligand, proton shuttle (general acid/base) |
M | ARG457 | electrostatic stabiliser |
M | HIS460 | metal ligand |
M | HIS462 | metal ligand |
site_id | MCSA2 |
Number of Residues | 5 |
Details | M-CSA 936 |
Chain | Residue | Details |
N | TYR408 | metal ligand |
N | HIS447 | metal ligand, proton shuttle (general acid/base) |
N | ARG457 | electrostatic stabiliser |
N | HIS460 | metal ligand |
N | HIS462 | metal ligand |
site_id | MCSA3 |
Number of Residues | 5 |
Details | M-CSA 936 |
Chain | Residue | Details |
O | TYR408 | metal ligand |
O | HIS447 | metal ligand, proton shuttle (general acid/base) |
O | ARG457 | electrostatic stabiliser |
O | HIS460 | metal ligand |
O | HIS462 | metal ligand |
site_id | MCSA4 |
Number of Residues | 5 |
Details | M-CSA 936 |
Chain | Residue | Details |
P | TYR408 | metal ligand |
P | HIS447 | metal ligand, proton shuttle (general acid/base) |
P | ARG457 | electrostatic stabiliser |
P | HIS460 | metal ligand |
P | HIS462 | metal ligand |
site_id | MCSA5 |
Number of Residues | 5 |
Details | M-CSA 936 |
Chain | Residue | Details |
Q | TYR408 | metal ligand |
Q | HIS447 | metal ligand, proton shuttle (general acid/base) |
Q | ARG457 | electrostatic stabiliser |
Q | HIS460 | metal ligand |
Q | HIS462 | metal ligand |
site_id | MCSA6 |
Number of Residues | 5 |
Details | M-CSA 936 |
Chain | Residue | Details |
R | TYR408 | metal ligand |
R | HIS447 | metal ligand, proton shuttle (general acid/base) |
R | ARG457 | electrostatic stabiliser |
R | HIS460 | metal ligand |
R | HIS462 | metal ligand |