4FAS
Complex crystal structure of hydroxylamine oxidoreductase and NE1300 from Nitrosomonas europaea
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019331 | biological_process | anaerobic respiration, using ammonium as electron donor |
| A | 0020037 | molecular_function | heme binding |
| A | 0033740 | molecular_function | hydroxylamine oxidoreductase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0044222 | cellular_component | anammoxosome |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047991 | molecular_function | hydroxylamine oxidase activity |
| A | 0070207 | biological_process | protein homotrimerization |
| A | 0140305 | molecular_function | hydroxylamine dehydrogenase activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019331 | biological_process | anaerobic respiration, using ammonium as electron donor |
| B | 0020037 | molecular_function | heme binding |
| B | 0033740 | molecular_function | hydroxylamine oxidoreductase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0044222 | cellular_component | anammoxosome |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047991 | molecular_function | hydroxylamine oxidase activity |
| B | 0070207 | biological_process | protein homotrimerization |
| B | 0140305 | molecular_function | hydroxylamine dehydrogenase activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0019331 | biological_process | anaerobic respiration, using ammonium as electron donor |
| C | 0020037 | molecular_function | heme binding |
| C | 0033740 | molecular_function | hydroxylamine oxidoreductase activity |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0044222 | cellular_component | anammoxosome |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0047991 | molecular_function | hydroxylamine oxidase activity |
| C | 0070207 | biological_process | protein homotrimerization |
| C | 0140305 | molecular_function | hydroxylamine dehydrogenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE HEC A 601 |
| Chain | Residue |
| A | TYR57 |
| A | HIS149 |
| A | HIS160 |
| A | ILE164 |
| A | MET166 |
| A | HEC602 |
| A | HOH798 |
| A | HOH929 |
| C | SER365 |
| C | GLU366 |
| C | ARG367 |
| A | TYR64 |
| A | ALA74 |
| A | ASP78 |
| A | CYS79 |
| A | CYS82 |
| A | HIS83 |
| A | GLU86 |
| A | CYS145 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEC A 602 |
| Chain | Residue |
| A | TYR57 |
| A | PRO60 |
| A | HIS83 |
| A | TRP90 |
| A | HIS99 |
| A | VAL143 |
| A | GLY144 |
| A | CYS145 |
| A | CYS148 |
| A | HIS149 |
| A | MET166 |
| A | PRO167 |
| A | LYS238 |
| A | ASP240 |
| A | ARG245 |
| A | HIS246 |
| A | PHE248 |
| A | HEC601 |
| A | HEC603 |
| C | HIS364 |
| C | SER365 |
| C | HOH783 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE HEC A 603 |
| Chain | Residue |
| A | THR98 |
| A | HIS99 |
| A | LYS117 |
| A | LYS120 |
| A | VAL143 |
| A | VAL152 |
| A | CYS172 |
| A | CYS175 |
| A | HIS176 |
| A | CYS239 |
| A | PHE248 |
| A | SER249 |
| A | ALA250 |
| A | HEC602 |
| A | HEC604 |
| A | HOH914 |
| site_id | AC4 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEC A 604 |
| Chain | Residue |
| A | TYR116 |
| A | LYS117 |
| A | CYS172 |
| A | HIS176 |
| A | GLU179 |
| A | HIS204 |
| A | ASN235 |
| A | CYS239 |
| A | CYS242 |
| A | HIS243 |
| A | SER253 |
| A | ARG254 |
| A | ARG295 |
| A | LEU296 |
| A | MET315 |
| A | HIS323 |
| A | HEC603 |
| A | HEC605 |
| A | HOH741 |
| A | HOH847 |
| A | HOH867 |
| site_id | AC5 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEC A 605 |
| Chain | Residue |
| C | ISW601 |
| A | PRO202 |
| A | SER203 |
| A | HIS204 |
| A | ASP207 |
| A | ALA210 |
| A | CYS232 |
| A | HIS233 |
| A | ASN235 |
| A | ASN241 |
| A | CYS242 |
| A | CYS259 |
| A | CYS262 |
| A | HIS263 |
| A | CYS310 |
| A | HIS314 |
| A | ILE325 |
| A | THR329 |
| A | ALA332 |
| A | HEC604 |
| A | HEC606 |
| A | HOH841 |
| site_id | AC6 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEC A 606 |
| Chain | Residue |
| A | HIS263 |
| A | ASN270 |
| A | TYR274 |
| A | HIS279 |
| A | THR309 |
| A | CYS310 |
| A | CYS313 |
| A | HIS314 |
| A | THR329 |
| A | ARG330 |
| A | TRP331 |
| A | ALA332 |
| A | TRP356 |
| A | MET376 |
| A | ALA458 |
| A | HIS459 |
| A | HEC605 |
| A | HOH724 |
| A | HOH797 |
| A | HOH851 |
| C | ISW601 |
| site_id | AC7 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEC A 607 |
| Chain | Residue |
| A | HIS279 |
| A | LEU282 |
| A | PHE300 |
| A | ASN306 |
| A | ALA307 |
| A | PRO308 |
| A | THR359 |
| A | CYS360 |
| A | CYS363 |
| A | HIS364 |
| A | PHE368 |
| A | TYR372 |
| A | VAL460 |
| A | HOH801 |
| A | HOH819 |
| B | TRP90 |
| B | LYS238 |
| B | ASP240 |
| B | THR244 |
| B | ARG245 |
| B | HOH734 |
| site_id | AC8 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE ISW A 608 |
| Chain | Residue |
| A | GLY463 |
| A | THR466 |
| A | TYR467 |
| A | HOH717 |
| B | TRP197 |
| B | ARG201 |
| B | ALA210 |
| B | ASN211 |
| B | THR214 |
| B | TRP217 |
| B | GLY228 |
| B | CYS229 |
| B | CYS232 |
| B | HIS233 |
| B | CYS262 |
| B | HIS263 |
| B | HIS268 |
| B | ASN333 |
| B | TYR334 |
| B | PHE428 |
| B | HEC605 |
| B | HEC606 |
| B | EDO621 |
| B | HOH765 |
| B | HOH782 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PEG A 609 |
| Chain | Residue |
| A | PHE63 |
| A | HOH932 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG A 610 |
| Chain | Residue |
| A | HIS38 |
| A | GLY39 |
| A | HOH758 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG A 611 |
| Chain | Residue |
| A | ASN449 |
| A | GLU469 |
| A | PRO473 |
| A | ARG476 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG A 612 |
| Chain | Residue |
| A | SER110 |
| A | ASP112 |
| A | PRO113 |
| A | LYS302 |
| A | EDO617 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG A 613 |
| Chain | Residue |
| A | TYR398 |
| A | GLU399 |
| A | GLN406 |
| A | LYS407 |
| A | HOH935 |
| site_id | BC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE PEG A 614 |
| Chain | Residue |
| C | ISW601 |
| site_id | BC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PGE A 615 |
| Chain | Residue |
| A | ARG96 |
| A | ASN101 |
| A | LYS104 |
| site_id | BC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 616 |
| Chain | Residue |
| A | ASP16 |
| A | ALA20 |
| A | GLU24 |
| site_id | BC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 617 |
| Chain | Residue |
| A | LYS302 |
| A | PEG612 |
| C | GLY132 |
| site_id | BC9 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO A 618 |
| Chain | Residue |
| B | ALA53 |
| site_id | CC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 619 |
| Chain | Residue |
| A | THR215 |
| A | PRO416 |
| A | LYS418 |
| site_id | CC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE HEC B 601 |
| Chain | Residue |
| A | SER365 |
| A | GLU366 |
| A | ARG367 |
| B | TYR57 |
| B | TYR64 |
| B | PRO70 |
| B | ASP78 |
| B | CYS79 |
| B | CYS82 |
| B | HIS83 |
| B | GLU86 |
| B | HIS149 |
| B | HIS160 |
| B | ILE164 |
| B | HEC602 |
| B | HOH710 |
| site_id | CC3 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEC B 602 |
| Chain | Residue |
| A | HIS364 |
| A | SER365 |
| A | HOH801 |
| B | TYR57 |
| B | PRO60 |
| B | HIS83 |
| B | TRP90 |
| B | HIS99 |
| B | VAL143 |
| B | GLY144 |
| B | CYS145 |
| B | CYS148 |
| B | HIS149 |
| B | MET166 |
| B | PRO167 |
| B | LYS238 |
| B | ASP240 |
| B | ARG245 |
| B | HIS246 |
| B | PHE248 |
| B | HEC601 |
| B | HEC603 |
| site_id | CC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE HEC B 603 |
| Chain | Residue |
| B | THR98 |
| B | HIS99 |
| B | LYS117 |
| B | LYS120 |
| B | LEU121 |
| B | VAL143 |
| B | CYS172 |
| B | CYS175 |
| B | HIS176 |
| B | CYS239 |
| B | PHE248 |
| B | ALA250 |
| B | HEC602 |
| B | HEC604 |
| B | HOH774 |
| site_id | CC5 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEC B 604 |
| Chain | Residue |
| B | TYR116 |
| B | LYS117 |
| B | CYS172 |
| B | HIS176 |
| B | GLU179 |
| B | HIS204 |
| B | ASN235 |
| B | CYS239 |
| B | CYS242 |
| B | HIS243 |
| B | SER253 |
| B | ARG254 |
| B | ARG295 |
| B | LEU296 |
| B | MET315 |
| B | HIS323 |
| B | HEC603 |
| B | HEC605 |
| B | HOH745 |
| B | HOH808 |
| B | HOH886 |
| site_id | CC6 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE HEC B 605 |
| Chain | Residue |
| A | ISW608 |
| B | ARG201 |
| B | PRO202 |
| B | SER203 |
| B | HIS204 |
| B | ASP207 |
| B | ALA210 |
| B | CYS232 |
| B | HIS233 |
| B | ASN235 |
| B | ASN241 |
| B | CYS242 |
| B | ALA258 |
| B | CYS259 |
| B | CYS262 |
| B | HIS263 |
| B | HIS314 |
| B | ILE325 |
| B | THR329 |
| B | ALA332 |
| B | HEC604 |
| B | HEC606 |
| B | HOH720 |
| site_id | CC7 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEC B 606 |
| Chain | Residue |
| A | ISW608 |
| B | HIS263 |
| B | ASN270 |
| B | TYR274 |
| B | HIS279 |
| B | PRO308 |
| B | THR309 |
| B | CYS310 |
| B | CYS313 |
| B | HIS314 |
| B | THR329 |
| B | ARG330 |
| B | TRP331 |
| B | ALA332 |
| B | TRP356 |
| B | MET376 |
| B | HIS459 |
| B | HEC605 |
| B | HEC607 |
| B | HOH761 |
| B | HOH881 |
| site_id | CC8 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE HEC B 607 |
| Chain | Residue |
| B | LYS278 |
| B | HIS279 |
| B | LEU282 |
| B | PHE300 |
| B | THR359 |
| B | CYS360 |
| B | CYS363 |
| B | HIS364 |
| B | PHE368 |
| B | TYR372 |
| B | VAL460 |
| B | HEC606 |
| B | HOH719 |
| B | HOH827 |
| C | LYS238 |
| C | ASP240 |
| C | THR244 |
| C | ARG245 |
| C | HOH710 |
| site_id | CC9 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE ISW B 608 |
| Chain | Residue |
| B | GLY463 |
| B | THR466 |
| B | TYR467 |
| B | HOH755 |
| C | TRP197 |
| C | ARG201 |
| C | ALA210 |
| C | ASN211 |
| C | THR214 |
| C | TRP217 |
| C | GLY228 |
| C | CYS229 |
| C | CYS232 |
| C | HIS233 |
| C | CYS262 |
| C | HIS263 |
| C | HIS268 |
| C | ASN333 |
| C | PHE428 |
| C | HEC606 |
| C | HEC607 |
| C | PEG610 |
| C | HOH711 |
| C | HOH743 |
| site_id | DC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG B 609 |
| Chain | Residue |
| B | THR98 |
| B | ASN101 |
| B | LYS104 |
| site_id | DC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG B 610 |
| Chain | Residue |
| B | SER3 |
| B | VAL5 |
| B | PG4614 |
| B | HOH905 |
| site_id | DC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG B 611 |
| Chain | Residue |
| B | PRO51 |
| B | ILE52 |
| B | PHE63 |
| site_id | DC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG B 612 |
| Chain | Residue |
| B | PHE336 |
| B | TYR387 |
| B | ASN391 |
| B | GLY422 |
| B | HOH837 |
| site_id | DC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE P6G B 613 |
| Chain | Residue |
| A | VAL73 |
| A | GLU75 |
| A | GLU81 |
| B | TYR116 |
| B | GLY119 |
| B | GLU123 |
| B | HOH760 |
| B | HOH877 |
| site_id | DC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PG4 B 614 |
| Chain | Residue |
| A | TRP94 |
| A | LYS95 |
| B | ASP1 |
| B | ARG17 |
| B | PEG610 |
| site_id | DC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO B 615 |
| Chain | Residue |
| B | SER371 |
| site_id | DC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO B 616 |
| Chain | Residue |
| B | GLU366 |
| site_id | DC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NO3 B 617 |
| Chain | Residue |
| B | ASP16 |
| B | GLU24 |
| site_id | EC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NO3 B 618 |
| Chain | Residue |
| B | SER130 |
| B | GLY132 |
| site_id | EC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO B 620 |
| Chain | Residue |
| B | GLU399 |
| B | LYS407 |
| site_id | EC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 621 |
| Chain | Residue |
| A | ISW608 |
| B | PHE424 |
| B | GLU447 |
| site_id | EC4 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE ISW C 601 |
| Chain | Residue |
| A | TRP197 |
| A | ARG201 |
| A | ALA210 |
| A | THR214 |
| A | TRP217 |
| A | GLY228 |
| A | CYS229 |
| A | CYS232 |
| A | HIS233 |
| A | THR261 |
| A | CYS262 |
| A | HIS263 |
| A | HIS268 |
| A | ASN333 |
| A | PHE428 |
| A | HEC605 |
| A | HEC606 |
| A | PEG614 |
| A | HOH721 |
| A | HOH746 |
| C | GLY463 |
| C | THR466 |
| C | TYR467 |
| C | HOH709 |
| site_id | EC5 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEC C 602 |
| Chain | Residue |
| A | GLU136 |
| B | SER365 |
| B | GLU366 |
| B | ARG367 |
| C | TYR57 |
| C | TYR64 |
| C | SER69 |
| C | GLU72 |
| C | ASP78 |
| C | CYS79 |
| C | CYS82 |
| C | HIS83 |
| C | GLU86 |
| C | HIS149 |
| C | HIS160 |
| C | HEC603 |
| C | HOH756 |
| C | HOH911 |
| site_id | EC6 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEC C 603 |
| Chain | Residue |
| B | HIS364 |
| B | SER365 |
| C | TYR57 |
| C | PRO60 |
| C | HIS83 |
| C | TRP90 |
| C | HIS99 |
| C | VAL143 |
| C | GLY144 |
| C | CYS145 |
| C | CYS148 |
| C | HIS149 |
| C | MET166 |
| C | PRO167 |
| C | ASP240 |
| C | ARG245 |
| C | HIS246 |
| C | PHE248 |
| C | HEC602 |
| C | HEC604 |
| site_id | EC7 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HEC C 604 |
| Chain | Residue |
| C | THR98 |
| C | HIS99 |
| C | LYS117 |
| C | LYS120 |
| C | LEU121 |
| C | VAL143 |
| C | VAL152 |
| C | CYS172 |
| C | CYS175 |
| C | HIS176 |
| C | CYS239 |
| C | PHE248 |
| C | SER249 |
| C | ALA250 |
| C | HEC603 |
| C | HEC605 |
| C | HOH770 |
| site_id | EC8 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEC C 605 |
| Chain | Residue |
| C | TYR116 |
| C | LYS117 |
| C | LYS120 |
| C | CYS172 |
| C | HIS176 |
| C | GLU179 |
| C | HIS204 |
| C | ASN235 |
| C | CYS239 |
| C | CYS242 |
| C | HIS243 |
| C | SER253 |
| C | ARG254 |
| C | ARG295 |
| C | LEU296 |
| C | MET315 |
| C | HIS323 |
| C | HEC604 |
| C | HEC606 |
| C | HOH781 |
| C | HOH897 |
| C | HOH916 |
| site_id | EC9 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEC C 606 |
| Chain | Residue |
| B | ISW608 |
| C | PRO202 |
| C | SER203 |
| C | HIS204 |
| C | ASP207 |
| C | ALA210 |
| C | CYS232 |
| C | HIS233 |
| C | ASN235 |
| C | ASN241 |
| C | ALA258 |
| C | CYS259 |
| C | CYS262 |
| C | HIS263 |
| C | HIS314 |
| C | ILE325 |
| C | THR329 |
| C | ALA332 |
| C | HEC605 |
| C | HEC607 |
| C | HOH918 |
| site_id | FC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEC C 607 |
| Chain | Residue |
| B | ISW608 |
| C | HIS263 |
| C | ASN270 |
| C | TYR274 |
| C | HIS279 |
| C | PRO308 |
| C | THR309 |
| C | CYS310 |
| C | CYS313 |
| C | HIS314 |
| C | THR329 |
| C | ARG330 |
| C | TRP331 |
| C | ALA332 |
| C | TRP356 |
| C | MET376 |
| C | ALA458 |
| C | HIS459 |
| C | HEC606 |
| C | HEC608 |
| C | HOH730 |
| C | HOH776 |
| site_id | FC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE HEC C 608 |
| Chain | Residue |
| A | TRP90 |
| A | LYS238 |
| A | ASP240 |
| A | THR244 |
| A | ARG245 |
| C | LYS278 |
| C | HIS279 |
| C | LEU282 |
| C | PHE300 |
| C | PRO308 |
| C | CYS360 |
| C | CYS363 |
| C | HIS364 |
| C | PHE368 |
| C | TYR372 |
| C | VAL460 |
| C | HEC607 |
| C | HOH763 |
| C | HOH783 |
| site_id | FC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG C 609 |
| Chain | Residue |
| C | GLY119 |
| C | GLU122 |
| C | ASN126 |
| site_id | FC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG C 610 |
| Chain | Residue |
| B | ISW608 |
| C | PHE424 |
| C | GLU447 |
| site_id | FC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG C 611 |
| Chain | Residue |
| A | ARG295 |
| A | LYS297 |
| A | GLU320 |
| C | GLY132 |
| C | GLU138 |
| site_id | FC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PEG C 612 |
| Chain | Residue |
| C | ARG76 |
| C | LYS141 |
| site_id | FC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG C 613 |
| Chain | Residue |
| C | ASP354 |
| C | LEU358 |
| C | THR361 |
| C | GLU366 |
| site_id | FC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PGE C 614 |
| Chain | Residue |
| C | ARG96 |
| C | THR98 |
| C | ASN101 |
| C | LYS104 |
| C | HOH928 |
| site_id | FC9 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO C 615 |
| Chain | Residue |
| C | ALA100 |
| site_id | GC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO C 616 |
| Chain | Residue |
| C | ARG370 |
| site_id | GC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO C 617 |
| Chain | Residue |
| B | LYS95 |
| C | LYS19 |
| site_id | GC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO C 618 |
| Chain | Residue |
| C | TYR398 |
| C | GLN406 |
| C | LYS407 |
| site_id | GC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NO3 C 619 |
| Chain | Residue |
| C | LYS289 |
| C | TRP290 |
| site_id | GC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO C 620 |
| Chain | Residue |
| C | PRO51 |
| site_id | GC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO C 621 |
| Chain | Residue |
| C | ALA37 |
| site_id | GC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG C 622 |
| Chain | Residue |
| C | SER110 |
| C | ASP112 |
| C | PRO113 |
| C | LYS302 |
| site_id | GC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE NO3 F 101 |
| Chain | Residue |
| F | LYS25 |
| site_id | GC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG F 102 |
| Chain | Residue |
| A | GLU50 |
| F | VAL30 |
| F | ARG44 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 48 |
| Details | Binding site: {"description":"covalent","evidences":[{"source":"PubMed","id":"24302732","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9095195","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1FGJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4N4N","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4N4O","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 45 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"24302732","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9095195","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1FGJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4N4N","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4N4O","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"24302732","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4N4O","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Binding site: {"description":"covalent; ligand shared between tetrameric partners","evidences":[{"source":"PubMed","id":"24302732","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 581 |
| Chain | Residue | Details |
| A | HIS233 | electrostatic stabiliser |
| A | ASP267 | steric role |
| A | HIS268 | steric role |
| A | TYR334 | steric role |
| A | TYR467 | activator, covalently attached |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 581 |
| Chain | Residue | Details |
| B | HIS233 | electrostatic stabiliser |
| B | ASP267 | steric role |
| B | HIS268 | steric role |
| B | TYR334 | steric role |
| B | TYR467 | activator, covalently attached |
| site_id | MCSA3 |
| Number of Residues | 5 |
| Details | M-CSA 581 |
| Chain | Residue | Details |
| C | HIS233 | electrostatic stabiliser |
| C | ASP267 | steric role |
| C | HIS268 | steric role |
| C | TYR334 | steric role |
| C | TYR467 | activator, covalently attached |
