1H7X
Dihydropyrimidine dehydrogenase (DPD) from pig, ternary complex of a mutant enzyme (C671A), NADPH and 5-fluorouracil
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0050661 | molecular_function | NADP binding |
| A | 0051536 | molecular_function | iron-sulfur cluster 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 | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0050661 | molecular_function | NADP binding |
| B | 0051536 | molecular_function | iron-sulfur cluster 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 | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0050661 | molecular_function | NADP binding |
| C | 0051536 | molecular_function | iron-sulfur cluster 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 | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| D | 0050661 | molecular_function | NADP binding |
| D | 0051536 | molecular_function | iron-sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SF4 A1026 |
| Chain | Residue |
| A | CYS91 |
| A | PRO92 |
| A | LEU95 |
| A | ILE97 |
| A | ASN120 |
| A | CYS130 |
| A | CYS136 |
| A | GLN156 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SF4 A1027 |
| Chain | Residue |
| A | LEU80 |
| A | LYS81 |
| A | CYS82 |
| A | PRO86 |
| A | CYS87 |
| A | CYS140 |
| A | ASN141 |
| A | LEU142 |
| A | ILE150 |
| A | ILE152 |
| A | CYS79 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SF4 A1028 |
| Chain | Residue |
| A | ILE948 |
| A | CYS953 |
| A | ILE954 |
| A | ASN955 |
| A | CYS956 |
| A | GLY957 |
| A | CYS959 |
| A | CYS996 |
| A | PRO997 |
| A | CYS1001 |
| 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 | 7 |
| Details | BINDING SITE FOR RESIDUE SF4 B1026 |
| Chain | Residue |
| B | CYS91 |
| B | PRO92 |
| B | ILE97 |
| B | ASN120 |
| B | CYS130 |
| B | CYS136 |
| B | GLN156 |
| site_id | AC6 |
| 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 | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SF4 B1028 |
| Chain | Residue |
| B | ILE948 |
| B | CYS953 |
| B | ILE954 |
| B | CYS956 |
| B | GLY957 |
| B | CYS959 |
| B | CYS996 |
| B | PRO997 |
| B | CYS1001 |
| B | ILE1002 |
| site_id | AC8 |
| 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 | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SF4 C1026 |
| Chain | Residue |
| C | CYS91 |
| C | PRO92 |
| C | LEU95 |
| C | ILE97 |
| C | ASN120 |
| C | CYS130 |
| C | CYS136 |
| C | GLN156 |
| site_id | BC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SF4 C1027 |
| Chain | Residue |
| C | CYS79 |
| C | LEU80 |
| C | LYS81 |
| C | CYS82 |
| C | PRO86 |
| C | CYS87 |
| C | CYS140 |
| C | ASN141 |
| C | LEU142 |
| C | ILE150 |
| C | ILE152 |
| site_id | BC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE SF4 C1028 |
| Chain | Residue |
| C | ASN955 |
| C | CYS956 |
| C | GLY957 |
| C | LYS958 |
| C | CYS959 |
| C | CYS996 |
| C | PRO997 |
| C | CYS1001 |
| C | ILE1002 |
| C | ILE948 |
| C | CYS953 |
| C | ILE954 |
| site_id | BC3 |
| 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 | BC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SF4 D1026 |
| Chain | Residue |
| D | CYS91 |
| D | PRO92 |
| D | ILE97 |
| D | ASN120 |
| D | CYS130 |
| D | LEU135 |
| D | CYS136 |
| D | GLN156 |
| site_id | BC5 |
| Number of Residues | 25 |
| 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 | THR735 |
| A | ASN736 |
| A | SER766 |
| A | GLY767 |
| A | THR793 |
| A | GLY794 |
| A | GLY795 |
| A | CYS816 |
| A | SER817 |
| A | GLN820 |
| A | URF1033 |
| A | HOH2750 |
| A | HOH2773 |
| A | HOH3033 |
| A | HOH3034 |
| site_id | BC6 |
| Number of Residues | 38 |
| Details | BINDING SITE FOR RESIDUE FAD A1031 |
| Chain | Residue |
| A | VAL129 |
| A | GLY194 |
| A | GLY196 |
| A | PRO197 |
| A | ALA198 |
| A | GLU218 |
| A | LYS219 |
| A | GLN220 |
| A | GLY225 |
| A | LEU226 |
| A | GLU230 |
| A | ARG235 |
| A | LYS259 |
| A | SER260 |
| A | LEU261 |
| A | GLY282 |
| A | ILE283 |
| A | GLY284 |
| A | PRO286 |
| A | LEU310 |
| A | THR343 |
| A | ASP346 |
| A | GLY480 |
| A | ASP481 |
| A | THR488 |
| A | THR489 |
| A | SER492 |
| A | NDP1032 |
| A | HOH2342 |
| A | HOH2512 |
| A | HOH3035 |
| A | HOH3037 |
| A | HOH3038 |
| A | HOH3039 |
| A | HOH3040 |
| A | HOH3041 |
| A | HOH3042 |
| A | HOH3043 |
| site_id | BC7 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NDP A1032 |
| Chain | Residue |
| A | ASP291 |
| A | GLY339 |
| A | ALA340 |
| A | GLY341 |
| A | ASP342 |
| A | THR343 |
| A | ARG364 |
| A | LYS365 |
| A | ARG371 |
| A | PRO393 |
| A | ALA437 |
| A | PHE438 |
| A | ASP481 |
| A | ALA486 |
| A | ASN487 |
| A | FAD1031 |
| A | HOH2469 |
| A | HOH2526 |
| A | HOH3039 |
| A | HOH3044 |
| A | HOH3045 |
| A | HOH3046 |
| A | HOH3047 |
| A | HOH3050 |
| A | HOH3051 |
| A | HOH3052 |
| site_id | BC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE URF A1033 |
| Chain | Residue |
| A | ASN609 |
| A | GLU611 |
| A | ILE613 |
| A | ASN668 |
| A | SER670 |
| A | ASN736 |
| A | THR737 |
| A | FMN1030 |
| site_id | BC9 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE FMN B1030 |
| Chain | Residue |
| B | ALA549 |
| B | SER550 |
| B | ALA551 |
| B | LYS574 |
| B | THR575 |
| B | ILE590 |
| B | ASN609 |
| B | GLU611 |
| B | ASN668 |
| B | LYS709 |
| B | THR735 |
| B | ASN736 |
| B | SER766 |
| B | GLY767 |
| B | THR793 |
| B | GLY794 |
| B | GLY795 |
| B | CYS816 |
| B | SER817 |
| B | GLN820 |
| B | URF1033 |
| B | HOH2753 |
| B | HOH2813 |
| B | HOH2830 |
| B | HOH3032 |
| site_id | CC1 |
| Number of Residues | 39 |
| Details | BINDING SITE FOR RESIDUE FAD B1031 |
| Chain | Residue |
| B | VAL129 |
| B | GLY194 |
| B | GLY196 |
| B | PRO197 |
| B | ALA198 |
| B | GLU218 |
| B | LYS219 |
| B | GLN220 |
| B | GLY225 |
| B | LEU226 |
| B | GLU230 |
| B | ARG235 |
| B | LYS259 |
| B | SER260 |
| B | LEU261 |
| B | GLY282 |
| B | ILE283 |
| B | GLY284 |
| B | PRO286 |
| B | LEU310 |
| B | THR343 |
| B | ASP346 |
| B | GLY480 |
| B | ASP481 |
| B | THR488 |
| B | THR489 |
| B | SER492 |
| B | NDP1032 |
| B | HOH2317 |
| B | HOH2390 |
| B | HOH2506 |
| B | HOH3033 |
| B | HOH3034 |
| B | HOH3035 |
| B | HOH3036 |
| B | HOH3037 |
| B | HOH3038 |
| B | HOH3039 |
| B | HOH3040 |
| site_id | CC2 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NDP B1032 |
| Chain | Residue |
| B | ASP291 |
| B | ALA340 |
| B | ASP342 |
| B | THR343 |
| B | ARG364 |
| B | LYS365 |
| B | ARG371 |
| B | PRO393 |
| B | ALA437 |
| B | PHE438 |
| B | ASP481 |
| B | GLY484 |
| B | MET485 |
| B | ALA486 |
| B | ASN487 |
| B | FAD1031 |
| B | HOH2499 |
| B | HOH2547 |
| B | HOH2550 |
| B | HOH3040 |
| B | HOH3041 |
| B | HOH3042 |
| B | HOH3044 |
| B | HOH3045 |
| B | HOH3046 |
| B | HOH3047 |
| site_id | CC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE URF B1033 |
| Chain | Residue |
| B | ASN609 |
| B | GLU611 |
| B | ILE613 |
| B | ASN668 |
| B | SER670 |
| B | ASN736 |
| B | THR737 |
| B | FMN1030 |
| site_id | CC4 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE FMN C1030 |
| Chain | Residue |
| C | ALA549 |
| C | SER550 |
| C | ALA551 |
| C | LYS574 |
| C | THR575 |
| C | ILE590 |
| C | ASN609 |
| C | GLU611 |
| C | ASN668 |
| C | LYS709 |
| C | THR735 |
| C | ASN736 |
| C | SER766 |
| C | GLY767 |
| C | THR793 |
| C | GLY794 |
| C | GLY795 |
| C | CYS816 |
| C | SER817 |
| C | GLN820 |
| C | URF1033 |
| C | HOH2770 |
| C | HOH2842 |
| C | HOH2857 |
| C | HOH2871 |
| C | HOH3080 |
| site_id | CC5 |
| Number of Residues | 37 |
| Details | BINDING SITE FOR RESIDUE FAD C1031 |
| Chain | Residue |
| C | VAL129 |
| C | PRO131 |
| C | GLY194 |
| C | GLY196 |
| C | PRO197 |
| C | ALA198 |
| C | GLU218 |
| C | LYS219 |
| C | GLN220 |
| C | GLY225 |
| C | LEU226 |
| C | GLU230 |
| C | ARG235 |
| C | SER260 |
| C | LEU261 |
| C | GLY282 |
| C | ILE283 |
| C | GLY284 |
| C | PRO286 |
| C | LEU310 |
| C | THR343 |
| C | ASP346 |
| C | GLY480 |
| C | ASP481 |
| C | THR488 |
| C | THR489 |
| C | SER492 |
| C | HOH2333 |
| C | HOH2514 |
| C | HOH2612 |
| C | HOH3081 |
| C | HOH3082 |
| C | HOH3083 |
| C | HOH3084 |
| C | HOH3085 |
| C | HOH3086 |
| C | HOH3087 |
| site_id | CC6 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE NDP C1032 |
| Chain | Residue |
| C | LYS289 |
| C | ASP291 |
| C | GLY339 |
| C | ALA340 |
| C | GLY341 |
| C | ASP342 |
| C | THR343 |
| C | ARG364 |
| C | LYS365 |
| C | ARG371 |
| C | ALA437 |
| C | PHE438 |
| C | GLY439 |
| C | HOH2480 |
| C | HOH3088 |
| C | HOH3089 |
| C | HOH3090 |
| C | HOH3093 |
| C | HOH3094 |
| C | HOH3095 |
| C | HOH3096 |
| site_id | CC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE URF C1033 |
| Chain | Residue |
| C | ASN609 |
| C | GLU611 |
| C | ILE613 |
| C | ASN668 |
| C | SER670 |
| C | ASN736 |
| C | THR737 |
| C | FMN1030 |
| 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 | 10 |
| Details | BINDING SITE FOR RESIDUE SF4 D1028 |
| Chain | Residue |
| D | ILE948 |
| D | CYS953 |
| D | ILE954 |
| D | CYS956 |
| D | GLY957 |
| 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 | 24 |
| Details | BINDING SITE FOR RESIDUE FMN D1030 |
| Chain | Residue |
| D | ALA549 |
| D | SER550 |
| D | ALA551 |
| D | LYS574 |
| D | THR575 |
| D | ILE590 |
| D | ASN609 |
| D | GLU611 |
| D | ASN668 |
| D | LYS709 |
| D | THR735 |
| D | ASN736 |
| D | SER766 |
| D | GLY767 |
| D | THR793 |
| D | GLY794 |
| D | GLY795 |
| D | CYS816 |
| D | SER817 |
| D | GLN820 |
| D | URF1033 |
| D | HOH2762 |
| D | HOH3072 |
| D | HOH3073 |
| site_id | DC3 |
| Number of Residues | 37 |
| Details | BINDING SITE FOR RESIDUE FAD D1031 |
| Chain | Residue |
| D | VAL129 |
| D | PRO131 |
| D | GLY194 |
| D | GLY196 |
| D | PRO197 |
| D | ALA198 |
| D | GLU218 |
| D | LYS219 |
| D | GLN220 |
| D | GLY225 |
| D | LEU226 |
| D | GLU230 |
| D | ARG235 |
| D | SER260 |
| D | LEU261 |
| D | GLY282 |
| D | ILE283 |
| D | GLY284 |
| D | PRO286 |
| D | LEU310 |
| D | THR343 |
| D | ASP346 |
| D | GLY480 |
| D | ASP481 |
| D | THR488 |
| D | THR489 |
| D | SER492 |
| D | HOH2358 |
| D | HOH2541 |
| D | HOH2622 |
| D | HOH2623 |
| D | HOH3074 |
| D | HOH3075 |
| D | HOH3076 |
| D | HOH3077 |
| D | HOH3078 |
| D | HOH3079 |
| site_id | DC4 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NDP D1032 |
| Chain | Residue |
| C | LYS47 |
| D | LYS289 |
| D | GLY339 |
| D | ALA340 |
| D | ASP342 |
| D | THR343 |
| D | ARG364 |
| D | LYS365 |
| D | ARG371 |
| D | PRO393 |
| D | ALA437 |
| D | PHE438 |
| D | ASN487 |
| D | THR488 |
| D | HOH2232 |
| D | HOH2534 |
| D | HOH2584 |
| D | HOH3081 |
| D | HOH3082 |
| D | HOH3083 |
| D | HOH3084 |
| D | HOH3085 |
| D | HOH3086 |
| D | HOH3087 |
| D | HOH3088 |
| D | HOH3089 |
| D | HOH3090 |
| D | HOH3091 |
| D | HOH3092 |
| D | HOH3093 |
| site_id | DC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE URF D1033 |
| Chain | Residue |
| D | ASN609 |
| D | GLU611 |
| D | ILE613 |
| D | ASN668 |
| D | SER670 |
| 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 | 124 |
| Details | Domain: {"description":"4Fe-4S ferredoxin-type 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 128 |
| Details | Domain: {"description":"4Fe-4S ferredoxin-type 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 116 |
| Details | Domain: {"description":"4Fe-4S ferredoxin-type 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"11796730","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 80 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 176 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11796730","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q12882","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | a catalytic site defined by CSA, PubMed 11179210, 9860876 |
| Chain | Residue | Details |
| A | ALA671 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | a catalytic site defined by CSA, PubMed 11179210, 9860876 |
| Chain | Residue | Details |
| B | ALA671 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | a catalytic site defined by CSA, PubMed 11179210, 9860876 |
| Chain | Residue | Details |
| C | ALA671 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | a catalytic site defined by CSA, PubMed 11179210, 9860876 |
| Chain | Residue | Details |
| D | ALA671 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 800 |
| Chain | Residue | Details |
| A | LYS574 | electrostatic stabiliser |
| A | ALA671 | 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 | ALA671 | 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 | ALA671 | 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 | ALA671 | proton acceptor, proton donor |
| D | LYS709 | electrostatic stabiliser |
