1TZL
Crystal Structure of Pyranose 2-Oxidase from the White-Rot Fungus Peniophora sp.
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
A | 0050233 | molecular_function | pyranose oxidase activity |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
B | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
B | 0050233 | molecular_function | pyranose oxidase activity |
B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
C | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
C | 0050233 | molecular_function | pyranose oxidase activity |
C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
D | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
D | 0050233 | molecular_function | pyranose oxidase activity |
D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
E | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
E | 0050233 | molecular_function | pyranose oxidase activity |
E | 0050660 | molecular_function | flavin adenine dinucleotide binding |
F | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
F | 0050233 | molecular_function | pyranose oxidase activity |
F | 0050660 | molecular_function | flavin adenine dinucleotide binding |
G | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
G | 0050233 | molecular_function | pyranose oxidase activity |
G | 0050660 | molecular_function | flavin adenine dinucleotide binding |
H | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
H | 0050233 | molecular_function | pyranose oxidase activity |
H | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 34 |
Details | BINDING SITE FOR RESIDUE FAD A 625 |
Chain | Residue |
A | VAL52 |
A | VAL160 |
A | GLY163 |
A | MSE164 |
A | HIS167 |
A | TRP168 |
A | THR169 |
A | CYS170 |
A | ALA171 |
A | VAL281 |
A | CYS283 |
A | GLY53 |
A | THR319 |
A | ALA320 |
A | HIS324 |
A | LEU547 |
A | ASN593 |
A | THR595 |
A | HOH626 |
A | HOH662 |
A | HOH665 |
A | HOH686 |
A | GLY55 |
A | HOH695 |
A | HOH722 |
A | HOH743 |
A | HOH792 |
A | HOH810 |
A | PRO56 |
A | ILE57 |
A | ASP76 |
A | ILE77 |
A | THR158 |
A | ARG159 |
site_id | AC2 |
Number of Residues | 36 |
Details | BINDING SITE FOR RESIDUE FAD B 625 |
Chain | Residue |
B | VAL52 |
B | GLY53 |
B | GLY55 |
B | PRO56 |
B | ILE57 |
B | ASP76 |
B | ILE77 |
B | THR158 |
B | ARG159 |
B | VAL160 |
B | GLY163 |
B | MSE164 |
B | HIS167 |
B | TRP168 |
B | THR169 |
B | CYS170 |
B | ALA171 |
B | VAL281 |
B | CYS283 |
B | THR319 |
B | ALA320 |
B | HIS324 |
B | LEU547 |
B | HIS548 |
B | ASN593 |
B | THR595 |
B | HOH649 |
B | HOH650 |
B | HOH656 |
B | HOH663 |
B | HOH688 |
B | HOH721 |
B | HOH796 |
B | HOH804 |
B | HOH811 |
B | HOH830 |
site_id | AC3 |
Number of Residues | 33 |
Details | BINDING SITE FOR RESIDUE FAD C 625 |
Chain | Residue |
C | HOH677 |
C | HOH687 |
C | HOH698 |
C | HOH756 |
C | VAL52 |
C | GLY53 |
C | GLY55 |
C | PRO56 |
C | ILE57 |
C | ASP76 |
C | ILE77 |
C | THR158 |
C | ARG159 |
C | VAL160 |
C | GLY163 |
C | MSE164 |
C | SER165 |
C | HIS167 |
C | TRP168 |
C | THR169 |
C | CYS170 |
C | ALA171 |
C | VAL281 |
C | CYS283 |
C | ALA320 |
C | HIS324 |
C | LEU547 |
C | ASN593 |
C | THR595 |
C | HOH626 |
C | HOH636 |
C | HOH641 |
C | HOH666 |
site_id | AC4 |
Number of Residues | 31 |
Details | BINDING SITE FOR RESIDUE FAD D 625 |
Chain | Residue |
D | VAL52 |
D | GLY53 |
D | GLY55 |
D | PRO56 |
D | ILE57 |
D | ASP76 |
D | ILE77 |
D | ILE107 |
D | THR158 |
D | ARG159 |
D | VAL160 |
D | GLY163 |
D | MSE164 |
D | HIS167 |
D | TRP168 |
D | THR169 |
D | CYS170 |
D | ALA171 |
D | VAL281 |
D | CYS283 |
D | ALA320 |
D | HIS324 |
D | LEU547 |
D | ASN593 |
D | THR595 |
D | HOH630 |
D | HOH631 |
D | HOH643 |
D | HOH681 |
D | HOH685 |
D | HOH752 |
site_id | AC5 |
Number of Residues | 34 |
Details | BINDING SITE FOR RESIDUE FAD E 625 |
Chain | Residue |
E | VAL52 |
E | GLY53 |
E | GLY55 |
E | PRO56 |
E | ILE57 |
E | ASP76 |
E | ILE77 |
E | THR158 |
E | ARG159 |
E | VAL160 |
E | GLY163 |
E | MSE164 |
E | HIS167 |
E | TRP168 |
E | THR169 |
E | CYS170 |
E | ALA171 |
E | VAL281 |
E | CYS283 |
E | THR319 |
E | ALA320 |
E | HIS324 |
E | LEU547 |
E | ASN593 |
E | THR595 |
E | HOH628 |
E | HOH629 |
E | HOH634 |
E | HOH636 |
E | HOH687 |
E | HOH743 |
E | HOH780 |
E | HOH783 |
E | HOH898 |
site_id | AC6 |
Number of Residues | 33 |
Details | BINDING SITE FOR RESIDUE FAD F 625 |
Chain | Residue |
F | GLY53 |
F | GLY55 |
F | PRO56 |
F | ILE57 |
F | ASP76 |
F | ILE77 |
F | THR158 |
F | ARG159 |
F | VAL160 |
F | GLY163 |
F | MSE164 |
F | HIS167 |
F | TRP168 |
F | THR169 |
F | ALA171 |
F | VAL281 |
F | CYS283 |
F | THR319 |
F | ALA320 |
F | HIS324 |
F | LEU547 |
F | ASN593 |
F | THR595 |
F | HOH632 |
F | HOH656 |
F | HOH661 |
F | HOH678 |
F | HOH683 |
F | HOH706 |
F | HOH719 |
F | HOH782 |
F | HOH814 |
F | HOH825 |
site_id | AC7 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE FAD G 625 |
Chain | Residue |
G | VAL52 |
G | GLY53 |
G | GLY55 |
G | PRO56 |
G | ILE57 |
G | ASP76 |
G | ILE77 |
G | THR158 |
G | ARG159 |
G | VAL160 |
G | GLY163 |
G | MSE164 |
G | HIS167 |
G | TRP168 |
G | THR169 |
G | ALA171 |
G | VAL281 |
G | CYS283 |
G | ALA320 |
G | HIS324 |
G | ASN593 |
G | THR595 |
G | HOH628 |
G | HOH629 |
G | HOH635 |
G | HOH680 |
G | HOH717 |
G | HOH723 |
G | HOH761 |
G | HOH813 |
site_id | AC8 |
Number of Residues | 34 |
Details | BINDING SITE FOR RESIDUE FAD H 625 |
Chain | Residue |
H | VAL52 |
H | GLY53 |
H | GLY55 |
H | PRO56 |
H | ILE57 |
H | ASP76 |
H | ILE77 |
H | THR158 |
H | ARG159 |
H | VAL160 |
H | GLY163 |
H | MSE164 |
H | HIS167 |
H | TRP168 |
H | THR169 |
H | CYS170 |
H | ALA171 |
H | VAL281 |
H | CYS283 |
H | ALA320 |
H | HIS324 |
H | LEU547 |
H | ASN593 |
H | THR595 |
H | HOH628 |
H | HOH653 |
H | HOH668 |
H | HOH689 |
H | HOH740 |
H | HOH742 |
H | HOH759 |
H | HOH775 |
H | HOH935 |
H | HOH938 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:E4QP00 |
Chain | Residue | Details |
A | HIS548 | |
B | HIS548 | |
C | HIS548 | |
D | HIS548 | |
E | HIS548 | |
F | HIS548 | |
G | HIS548 | |
H | HIS548 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | ACT_SITE: |
Chain | Residue | Details |
A | ASN593 | |
B | ASN593 | |
C | ASN593 | |
D | ASN593 | |
E | ASN593 | |
F | ASN593 | |
G | ASN593 | |
H | ASN593 |
site_id | SWS_FT_FI3 |
Number of Residues | 16 |
Details | BINDING: |
Chain | Residue | Details |
A | GLN448 | |
E | HIS450 | |
F | GLN448 | |
F | HIS450 | |
G | GLN448 | |
G | HIS450 | |
H | GLN448 | |
H | HIS450 | |
A | HIS450 | |
B | GLN448 | |
B | HIS450 | |
C | GLN448 | |
C | HIS450 | |
D | GLN448 | |
D | HIS450 | |
E | GLN448 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | MOD_RES: Tele-8alpha-FAD histidine |
Chain | Residue | Details |
A | HIS167 | |
B | HIS167 | |
C | HIS167 | |
D | HIS167 | |
E | HIS167 | |
F | HIS167 | |
G | HIS167 | |
H | HIS167 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1kdg |
Chain | Residue | Details |
A | ASN593 | |
A | HIS548 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1kdg |
Chain | Residue | Details |
B | ASN593 | |
B | HIS548 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1kdg |
Chain | Residue | Details |
C | ASN593 | |
C | HIS548 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1kdg |
Chain | Residue | Details |
D | ASN593 | |
D | HIS548 |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1kdg |
Chain | Residue | Details |
E | ASN593 | |
E | HIS548 |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1kdg |
Chain | Residue | Details |
F | ASN593 | |
F | HIS548 |
site_id | CSA7 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1kdg |
Chain | Residue | Details |
G | ASN593 | |
G | HIS548 |
site_id | CSA8 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1kdg |
Chain | Residue | Details |
H | ASN593 | |
H | HIS548 |