1GT8
DIHYDROPYRIMIDINE DEHYDROGENASE (DPD) FROM PIG, TERNARY COMPLEX WITH NADPH AND URACIL-4-ACETIC ACID
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0002058 | molecular_function | uracil binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006210 | biological_process | thymine catabolic process |
| A | 0006212 | biological_process | uracil catabolic process |
| A | 0006214 | biological_process | thymidine catabolic process |
| A | 0010181 | molecular_function | FMN binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| A | 0017113 | molecular_function | dihydropyrimidine dehydrogenase (NADP+) activity |
| A | 0019483 | biological_process | beta-alanine biosynthetic process |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0050661 | molecular_function | NADP binding |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0002058 | molecular_function | uracil binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006210 | biological_process | thymine catabolic process |
| B | 0006212 | biological_process | uracil catabolic process |
| B | 0006214 | biological_process | thymidine catabolic process |
| B | 0010181 | molecular_function | FMN binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| B | 0017113 | molecular_function | dihydropyrimidine dehydrogenase (NADP+) activity |
| B | 0019483 | biological_process | beta-alanine biosynthetic process |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0050661 | molecular_function | NADP binding |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0002058 | molecular_function | uracil binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0006210 | biological_process | thymine catabolic process |
| C | 0006212 | biological_process | uracil catabolic process |
| C | 0006214 | biological_process | thymidine catabolic process |
| C | 0010181 | molecular_function | FMN binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| C | 0017113 | molecular_function | dihydropyrimidine dehydrogenase (NADP+) activity |
| C | 0019483 | biological_process | beta-alanine biosynthetic process |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0050661 | molecular_function | NADP binding |
| C | 0051536 | molecular_function | iron-sulfur cluster binding |
| C | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0002058 | molecular_function | uracil binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0006210 | biological_process | thymine catabolic process |
| D | 0006212 | biological_process | uracil catabolic process |
| D | 0006214 | biological_process | thymidine catabolic process |
| D | 0010181 | molecular_function | FMN binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| D | 0017113 | molecular_function | dihydropyrimidine dehydrogenase (NADP+) activity |
| D | 0019483 | biological_process | beta-alanine biosynthetic process |
| D | 0042803 | molecular_function | protein homodimerization activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| D | 0050661 | molecular_function | NADP binding |
| D | 0051536 | molecular_function | iron-sulfur cluster binding |
| D | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SF4 A1026 |
| Chain | Residue |
| A | CYS91 |
| A | GLN156 |
| A | PRO92 |
| A | LEU95 |
| A | ILE97 |
| A | ASN120 |
| A | CYS130 |
| A | THR132 |
| A | LEU135 |
| A | CYS136 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SF4 A1027 |
| Chain | Residue |
| A | CYS79 |
| A | LEU80 |
| A | LYS81 |
| A | CYS82 |
| A | PRO86 |
| A | CYS87 |
| A | CYS140 |
| A | ASN141 |
| A | ILE150 |
| A | ILE152 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE SF4 A1028 |
| Chain | Residue |
| A | ILE948 |
| A | CYS953 |
| A | ILE954 |
| A | ASN955 |
| A | CYS956 |
| A | GLY957 |
| A | LYS958 |
| A | CYS959 |
| A | CYS996 |
| A | PRO997 |
| A | CYS1001 |
| A | ILE1002 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SF4 A1029 |
| Chain | Residue |
| A | CYS963 |
| A | TYR968 |
| A | ILE971 |
| A | VAL982 |
| A | CYS986 |
| A | THR987 |
| A | GLY988 |
| A | CYS989 |
| A | THR990 |
| A | CYS992 |
| site_id | AC5 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE FMN A1030 |
| Chain | Residue |
| A | ALA549 |
| A | SER550 |
| A | ALA551 |
| A | LYS574 |
| A | THR575 |
| A | ILE590 |
| A | ASN609 |
| A | GLU611 |
| A | ASN668 |
| A | LYS709 |
| A | THR737 |
| A | SER766 |
| A | GLY767 |
| A | THR793 |
| A | GLY794 |
| A | GLY795 |
| A | CYS816 |
| A | SER817 |
| A | GLN820 |
| A | UAA1035 |
| site_id | AC6 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE FAD A1031 |
| Chain | Residue |
| A | VAL129 |
| A | GLY194 |
| A | GLY196 |
| A | PRO197 |
| A | ALA198 |
| A | PHE217 |
| A | GLU218 |
| A | LYS219 |
| A | GLN220 |
| A | GLY225 |
| A | LEU226 |
| A | GLU230 |
| A | ILE231 |
| A | ARG235 |
| A | SER260 |
| A | LEU261 |
| A | ILE283 |
| A | LEU310 |
| A | THR343 |
| A | ASP346 |
| A | GLY480 |
| A | ASP481 |
| A | THR488 |
| A | THR489 |
| A | SER492 |
| A | NDP1032 |
| site_id | AC7 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE NDP A1032 |
| Chain | Residue |
| A | ASN487 |
| A | FAD1031 |
| A | PRO131 |
| A | ALA340 |
| A | GLY341 |
| A | ASP342 |
| A | THR343 |
| A | ARG364 |
| A | LYS365 |
| A | ARG371 |
| A | ALA437 |
| A | PHE438 |
| A | GLY439 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE UAA A1035 |
| Chain | Residue |
| A | ASN609 |
| A | GLU611 |
| A | LEU612 |
| A | ILE613 |
| A | ASN668 |
| A | SER670 |
| A | ASN736 |
| A | GLY764 |
| A | FMN1030 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 B1026 |
| Chain | Residue |
| B | CYS91 |
| B | PRO92 |
| B | LEU95 |
| B | ILE97 |
| B | ASN120 |
| B | CYS130 |
| B | THR132 |
| B | CYS136 |
| B | GLN156 |
| site_id | BC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SF4 B1027 |
| Chain | Residue |
| B | CYS79 |
| B | LEU80 |
| B | LYS81 |
| B | CYS82 |
| B | PRO86 |
| B | CYS87 |
| B | CYS140 |
| B | ASN141 |
| B | LEU142 |
| B | ILE150 |
| B | ILE152 |
| site_id | BC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SF4 B1028 |
| Chain | Residue |
| B | ILE948 |
| B | CYS953 |
| B | ILE954 |
| B | CYS956 |
| B | GLY957 |
| B | LYS958 |
| B | CYS959 |
| B | CYS996 |
| B | PRO997 |
| B | CYS1001 |
| B | ILE1002 |
| site_id | BC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SF4 B1029 |
| Chain | Residue |
| B | CYS963 |
| B | TYR968 |
| B | ILE971 |
| B | VAL982 |
| B | CYS986 |
| B | THR987 |
| B | GLY988 |
| B | CYS989 |
| B | THR990 |
| B | CYS992 |
| site_id | BC4 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE FMN B1030 |
| Chain | Residue |
| B | ALA549 |
| B | SER550 |
| B | ALA551 |
| B | LYS574 |
| B | THR575 |
| B | ILE590 |
| B | ASN609 |
| B | ASN668 |
| B | LYS709 |
| B | THR735 |
| B | ASN736 |
| B | THR737 |
| B | SER766 |
| B | GLY767 |
| B | THR793 |
| B | GLY794 |
| B | GLY795 |
| B | CYS816 |
| B | SER817 |
| B | GLN820 |
| B | UAA1035 |
| site_id | BC5 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE FAD B1031 |
| Chain | Residue |
| B | VAL129 |
| B | GLY194 |
| B | GLY196 |
| B | PRO197 |
| B | ALA198 |
| B | PHE217 |
| B | GLU218 |
| B | LYS219 |
| B | GLN220 |
| B | GLY225 |
| B | LEU226 |
| B | GLU230 |
| B | ILE231 |
| B | ARG235 |
| B | LYS259 |
| B | SER260 |
| B | LEU261 |
| B | ILE283 |
| B | LEU310 |
| B | THR343 |
| B | ASP346 |
| B | GLY480 |
| B | ASP481 |
| B | THR488 |
| B | THR489 |
| B | SER492 |
| B | NDP1032 |
| site_id | BC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE NDP B1032 |
| Chain | Residue |
| B | PRO131 |
| B | ALA340 |
| B | GLY341 |
| B | ASP342 |
| B | THR343 |
| B | ARG364 |
| B | LYS365 |
| B | ARG371 |
| B | PRO393 |
| B | ALA437 |
| B | PHE438 |
| B | GLY439 |
| B | ASN487 |
| B | FAD1031 |
| site_id | BC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE UAA B1035 |
| Chain | Residue |
| B | ASN609 |
| B | GLU611 |
| B | ILE613 |
| B | ASN668 |
| B | SER670 |
| B | ASN736 |
| B | THR737 |
| B | GLY764 |
| B | FMN1030 |
| site_id | BC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 C1026 |
| Chain | Residue |
| C | CYS91 |
| C | PRO92 |
| C | LEU95 |
| C | ILE97 |
| C | CYS130 |
| C | THR132 |
| C | LEU135 |
| C | CYS136 |
| C | GLN156 |
| site_id | BC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 C1027 |
| Chain | Residue |
| C | CYS79 |
| C | LEU80 |
| C | LYS81 |
| C | CYS82 |
| C | CYS87 |
| C | CYS140 |
| C | ASN141 |
| C | ILE150 |
| C | ILE152 |
| site_id | CC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SF4 C1028 |
| Chain | Residue |
| C | ILE948 |
| C | CYS953 |
| C | ILE954 |
| C | CYS956 |
| C | GLY957 |
| C | LYS958 |
| C | CYS959 |
| C | CYS996 |
| C | PRO997 |
| C | CYS1001 |
| C | ILE1002 |
| site_id | CC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SF4 C1029 |
| Chain | Residue |
| C | CYS963 |
| C | TYR968 |
| C | ILE971 |
| C | VAL982 |
| C | CYS986 |
| C | THR987 |
| C | GLY988 |
| C | CYS989 |
| C | THR990 |
| C | CYS992 |
| site_id | CC3 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE FMN C1030 |
| Chain | Residue |
| C | ALA549 |
| C | SER550 |
| C | ALA551 |
| C | LYS574 |
| C | THR575 |
| C | ILE590 |
| C | ASN609 |
| C | ASN668 |
| C | LYS709 |
| C | ASN736 |
| C | SER766 |
| C | GLY767 |
| C | THR793 |
| C | GLY794 |
| C | GLY795 |
| C | CYS816 |
| C | SER817 |
| C | GLN820 |
| C | UAA1035 |
| site_id | CC4 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE FAD C1031 |
| Chain | Residue |
| C | VAL129 |
| C | GLY194 |
| C | GLY196 |
| C | PRO197 |
| C | ALA198 |
| C | PHE217 |
| C | GLU218 |
| C | LYS219 |
| C | GLN220 |
| C | GLY225 |
| C | LEU226 |
| C | GLU230 |
| C | ILE231 |
| C | ARG235 |
| C | SER260 |
| C | LEU261 |
| C | GLY282 |
| C | ILE283 |
| C | LEU310 |
| C | THR343 |
| C | ASP346 |
| C | GLY480 |
| C | ASP481 |
| C | THR488 |
| C | THR489 |
| C | SER492 |
| C | NDP1032 |
| site_id | CC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE NDP C1032 |
| Chain | Residue |
| C | PRO131 |
| C | ALA340 |
| C | GLY341 |
| C | ASP342 |
| C | THR343 |
| C | ARG364 |
| C | LYS365 |
| C | ARG371 |
| C | ALA437 |
| C | PHE438 |
| C | GLY439 |
| C | ASN487 |
| C | THR488 |
| C | FAD1031 |
| site_id | CC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE UAA C1035 |
| Chain | Residue |
| C | ASN609 |
| C | GLU611 |
| C | LEU612 |
| C | ILE613 |
| C | ASN668 |
| C | SER670 |
| C | ASN736 |
| C | THR737 |
| C | GLY764 |
| C | FMN1030 |
| site_id | CC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 D1026 |
| Chain | Residue |
| D | CYS91 |
| D | PRO92 |
| D | LEU95 |
| D | ILE97 |
| D | ASN120 |
| D | CYS130 |
| D | THR132 |
| D | CYS136 |
| D | GLN156 |
| site_id | CC8 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SF4 D1027 |
| Chain | Residue |
| D | CYS79 |
| D | LEU80 |
| D | LYS81 |
| D | CYS82 |
| D | PRO86 |
| D | CYS87 |
| D | CYS140 |
| D | ASN141 |
| D | LEU142 |
| D | ILE150 |
| D | ILE152 |
| site_id | CC9 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SF4 D1028 |
| Chain | Residue |
| D | ILE948 |
| D | CYS953 |
| D | ILE954 |
| D | CYS956 |
| D | GLY957 |
| D | LYS958 |
| D | CYS959 |
| D | CYS996 |
| D | PRO997 |
| D | CYS1001 |
| D | ILE1002 |
| site_id | DC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SF4 D1029 |
| Chain | Residue |
| D | CYS963 |
| D | TYR968 |
| D | ILE971 |
| D | VAL982 |
| D | CYS986 |
| D | THR987 |
| D | GLY988 |
| D | CYS989 |
| D | THR990 |
| D | CYS992 |
| site_id | DC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE FMN D1030 |
| Chain | Residue |
| D | ALA549 |
| D | SER550 |
| D | ALA551 |
| D | LYS574 |
| D | THR575 |
| D | ILE590 |
| D | ASN609 |
| D | ASN668 |
| D | LYS709 |
| D | THR735 |
| D | THR737 |
| D | SER766 |
| D | GLY767 |
| D | THR793 |
| D | GLY794 |
| D | GLY795 |
| D | CYS816 |
| D | SER817 |
| D | GLN820 |
| D | UAA1035 |
| site_id | DC3 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE FAD D1031 |
| Chain | Residue |
| D | VAL129 |
| D | GLY194 |
| D | GLY196 |
| D | PRO197 |
| D | ALA198 |
| D | PHE217 |
| D | GLU218 |
| D | LYS219 |
| D | GLN220 |
| D | GLY225 |
| D | LEU226 |
| D | GLU230 |
| D | ILE231 |
| D | ARG235 |
| D | LYS259 |
| D | SER260 |
| D | LEU261 |
| D | ILE283 |
| D | LEU310 |
| D | THR343 |
| D | ASP346 |
| D | GLY480 |
| D | ASP481 |
| D | THR488 |
| D | THR489 |
| D | SER492 |
| D | NDP1032 |
| site_id | DC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE NDP D1032 |
| Chain | Residue |
| D | PRO131 |
| D | ALA340 |
| D | GLY341 |
| D | ASP342 |
| D | THR343 |
| D | ARG364 |
| D | LYS365 |
| D | ARG371 |
| D | PRO393 |
| D | ALA437 |
| D | PHE438 |
| D | GLY439 |
| D | ASN487 |
| D | THR488 |
| D | FAD1031 |
| site_id | DC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE UAA D1035 |
| Chain | Residue |
| D | ASN609 |
| D | GLU611 |
| D | ILE613 |
| D | ASN668 |
| D | ASN736 |
| D | THR737 |
| D | FMN1030 |
Functional Information from PROSITE/UniProt
| site_id | PS00198 |
| Number of Residues | 12 |
| Details | 4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CtGCTlCLsVCP |
| Chain | Residue | Details |
| A | CYS986-PRO997 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:11796730 |
| Chain | Residue | Details |
| A | CYS671 | |
| B | CYS671 | |
| C | CYS671 | |
| D | CYS671 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 76 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | CYS79 | |
| A | ASN668 | |
| A | ASN736 | |
| A | CYS953 | |
| A | CYS956 | |
| A | CYS959 | |
| A | CYS963 | |
| A | CYS986 | |
| A | CYS989 | |
| A | CYS992 | |
| A | CYS996 | |
| A | CYS82 | |
| B | CYS79 | |
| B | CYS82 | |
| B | CYS87 | |
| B | CYS91 | |
| B | CYS130 | |
| B | CYS136 | |
| B | CYS140 | |
| B | GLN156 | |
| B | ASN609 | |
| B | ASN668 | |
| A | CYS87 | |
| B | ASN736 | |
| B | CYS953 | |
| B | CYS956 | |
| B | CYS959 | |
| B | CYS963 | |
| B | CYS986 | |
| B | CYS989 | |
| B | CYS992 | |
| B | CYS996 | |
| C | CYS79 | |
| A | CYS91 | |
| C | CYS82 | |
| C | CYS87 | |
| C | CYS91 | |
| C | CYS130 | |
| C | CYS136 | |
| C | CYS140 | |
| C | GLN156 | |
| C | ASN609 | |
| C | ASN668 | |
| C | ASN736 | |
| A | CYS130 | |
| C | CYS953 | |
| C | CYS956 | |
| C | CYS959 | |
| C | CYS963 | |
| C | CYS986 | |
| C | CYS989 | |
| C | CYS992 | |
| C | CYS996 | |
| D | CYS79 | |
| D | CYS82 | |
| A | CYS136 | |
| D | CYS87 | |
| D | CYS91 | |
| D | CYS130 | |
| D | CYS136 | |
| D | CYS140 | |
| D | GLN156 | |
| D | ASN609 | |
| D | ASN668 | |
| D | ASN736 | |
| D | CYS953 | |
| A | CYS140 | |
| D | CYS956 | |
| D | CYS959 | |
| D | CYS963 | |
| D | CYS986 | |
| D | CYS989 | |
| D | CYS992 | |
| D | CYS996 | |
| A | GLN156 | |
| A | ASN609 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 68 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11796730 |
| Chain | Residue | Details |
| A | VAL129 | |
| A | GLY480 | |
| A | ASP481 | |
| A | SER550 | |
| A | LYS574 | |
| A | LYS709 | |
| A | GLY767 | |
| A | THR793 | |
| A | CYS816 | |
| B | VAL129 | |
| B | GLY194 | |
| A | GLY194 | |
| B | GLU218 | |
| B | ARG235 | |
| B | LEU261 | |
| B | ALA340 | |
| B | ARG364 | |
| B | ARG371 | |
| B | ALA437 | |
| B | GLY480 | |
| B | ASP481 | |
| B | SER550 | |
| A | GLU218 | |
| B | LYS574 | |
| B | LYS709 | |
| B | GLY767 | |
| B | THR793 | |
| B | CYS816 | |
| C | VAL129 | |
| C | GLY194 | |
| C | GLU218 | |
| C | ARG235 | |
| C | LEU261 | |
| A | ARG235 | |
| C | ALA340 | |
| C | ARG364 | |
| C | ARG371 | |
| C | ALA437 | |
| C | GLY480 | |
| C | ASP481 | |
| C | SER550 | |
| C | LYS574 | |
| C | LYS709 | |
| C | GLY767 | |
| A | LEU261 | |
| C | THR793 | |
| C | CYS816 | |
| D | VAL129 | |
| D | GLY194 | |
| D | GLU218 | |
| D | ARG235 | |
| D | LEU261 | |
| D | ALA340 | |
| D | ARG364 | |
| D | ARG371 | |
| A | ALA340 | |
| D | ALA437 | |
| D | GLY480 | |
| D | ASP481 | |
| D | SER550 | |
| D | LYS574 | |
| D | LYS709 | |
| D | GLY767 | |
| D | THR793 | |
| D | CYS816 | |
| A | ARG364 | |
| A | ARG371 | |
| A | ALA437 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q12882 |
| Chain | Residue | Details |
| A | LYS384 | |
| B | LYS384 | |
| C | LYS384 | |
| D | LYS384 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 800 |
| Chain | Residue | Details |
| A | LYS574 | electrostatic stabiliser |
| A | CYS671 | proton acceptor, proton donor |
| A | LYS709 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 800 |
| Chain | Residue | Details |
| B | LYS574 | electrostatic stabiliser |
| B | CYS671 | proton acceptor, proton donor |
| B | LYS709 | electrostatic stabiliser |
| site_id | MCSA3 |
| Number of Residues | 3 |
| Details | M-CSA 800 |
| Chain | Residue | Details |
| C | LYS574 | electrostatic stabiliser |
| C | CYS671 | proton acceptor, proton donor |
| C | LYS709 | electrostatic stabiliser |
| site_id | MCSA4 |
| Number of Residues | 3 |
| Details | M-CSA 800 |
| Chain | Residue | Details |
| D | LYS574 | electrostatic stabiliser |
| D | CYS671 | proton acceptor, proton donor |
| D | LYS709 | electrostatic stabiliser |
