1FGJ
X-RAY STRUCTURE OF HYDROXYLAMINE OXIDOREDUCTASE
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HEM A 547 |
| Chain | Residue |
| A | TYR57 |
| A | CYS145 |
| A | ILE146 |
| A | HIS149 |
| A | HIS160 |
| A | SER365 |
| A | GLU366 |
| A | ARG367 |
| A | HEM548 |
| A | TYR64 |
| A | PRO67 |
| A | SER69 |
| A | ALA74 |
| A | CYS79 |
| A | CYS82 |
| A | HIS83 |
| A | GLU86 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEM A 548 |
| Chain | Residue |
| A | TYR57 |
| A | PRO60 |
| A | HIS83 |
| A | TRP90 |
| A | TRP94 |
| 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 | HIS364 |
| A | SER365 |
| A | HEM547 |
| A | HEM549 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE HEM A 549 |
| Chain | Residue |
| A | THR98 |
| A | HIS99 |
| A | LYS117 |
| A | LYS120 |
| A | LEU121 |
| A | VAL143 |
| A | CYS172 |
| A | CYS175 |
| A | HIS176 |
| A | CYS239 |
| A | PHE248 |
| A | ALA250 |
| A | HEM548 |
| A | HEM551 |
| site_id | AC4 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE HEC A 550 |
| Chain | Residue |
| A | TRP197 |
| A | ARG201 |
| A | ALA210 |
| A | ASN211 |
| A | THR214 |
| A | GLY228 |
| A | CYS229 |
| A | CYS232 |
| A | HIS233 |
| A | THR261 |
| A | CYS262 |
| A | HIS263 |
| A | HIS268 |
| A | ALA332 |
| A | ASN333 |
| A | THR466 |
| A | TYR467 |
| A | HEM552 |
| A | HEM553 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEM A 551 |
| 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 | HEM549 |
| A | HEM552 |
| site_id | AC6 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEM A 552 |
| Chain | Residue |
| A | ASN241 |
| A | CYS242 |
| A | ALA258 |
| A | CYS259 |
| A | CYS262 |
| A | HIS263 |
| A | ILE325 |
| A | THR329 |
| A | HEC550 |
| A | HEM551 |
| A | HEM553 |
| A | PRO202 |
| A | SER203 |
| A | HIS204 |
| A | ASP207 |
| A | ALA210 |
| A | MET231 |
| A | CYS232 |
| A | HIS233 |
| A | ASN235 |
| site_id | AC7 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE HEM A 553 |
| Chain | Residue |
| A | HIS263 |
| A | ASN270 |
| A | TYR274 |
| A | THR309 |
| A | CYS310 |
| A | CYS313 |
| A | HIS314 |
| A | ARG330 |
| A | TRP331 |
| A | TRP356 |
| A | MET376 |
| A | HIS459 |
| A | HEC550 |
| A | HEM552 |
| A | HEM554 |
| site_id | AC8 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE HEM A 554 |
| Chain | Residue |
| A | TRP90 |
| A | MET231 |
| A | LYS238 |
| A | ASP240 |
| A | THR244 |
| A | ARG245 |
| A | HIS279 |
| A | PHE300 |
| A | ASN306 |
| A | ALA307 |
| A | PRO308 |
| A | THR359 |
| A | CYS360 |
| A | CYS363 |
| A | HIS364 |
| A | PHE368 |
| A | TYR372 |
| A | VAL460 |
| A | HEM553 |
| site_id | AC9 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE HEM B 547 |
| Chain | Residue |
| B | TYR57 |
| B | TYR64 |
| B | PRO67 |
| B | ALA74 |
| B | ASP78 |
| B | CYS79 |
| B | CYS82 |
| B | HIS83 |
| B | HIS149 |
| B | HIS160 |
| B | SER365 |
| B | GLU366 |
| B | ARG367 |
| B | HEM548 |
| site_id | BC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEM B 548 |
| Chain | Residue |
| B | TYR57 |
| 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 | HIS364 |
| B | SER365 |
| B | HEM547 |
| B | HEM549 |
| site_id | BC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE HEM B 549 |
| Chain | Residue |
| B | THR98 |
| B | HIS99 |
| B | LEU102 |
| B | LYS117 |
| B | LYS120 |
| B | LEU121 |
| B | VAL143 |
| B | CYS172 |
| B | CYS175 |
| B | HIS176 |
| B | CYS239 |
| B | PHE248 |
| B | ALA250 |
| B | HEM548 |
| B | HEM551 |
| site_id | BC3 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEC B 550 |
| Chain | Residue |
| B | TRP197 |
| B | ARG201 |
| B | ALA210 |
| B | ASN211 |
| B | THR214 |
| B | TRP217 |
| B | GLY228 |
| B | CYS229 |
| B | CYS232 |
| B | HIS233 |
| B | THR261 |
| B | CYS262 |
| B | HIS263 |
| B | HIS268 |
| B | ALA332 |
| B | ASN333 |
| B | THR466 |
| B | TYR467 |
| B | HEM552 |
| B | HEM553 |
| site_id | BC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HEM B 551 |
| Chain | Residue |
| B | TYR116 |
| B | LYS117 |
| B | CYS172 |
| B | HIS176 |
| B | GLU179 |
| B | ASN235 |
| B | CYS239 |
| B | CYS242 |
| B | HIS243 |
| B | SER253 |
| B | ARG254 |
| B | ARG295 |
| B | LEU296 |
| B | MET315 |
| B | HIS323 |
| B | HEM549 |
| B | HEM552 |
| site_id | BC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE HEM B 552 |
| Chain | Residue |
| B | PRO202 |
| B | SER203 |
| B | HIS204 |
| B | ALA210 |
| B | CYS232 |
| B | HIS233 |
| B | ASN235 |
| B | ASN241 |
| B | CYS259 |
| B | CYS262 |
| B | HIS263 |
| B | ALA332 |
| B | HEC550 |
| B | HEM551 |
| B | HEM553 |
| site_id | BC6 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEM B 553 |
| Chain | Residue |
| B | CYS259 |
| B | HIS263 |
| B | ASN270 |
| B | TRP271 |
| B | TYR274 |
| B | PRO308 |
| B | THR309 |
| B | CYS310 |
| B | CYS313 |
| B | HIS314 |
| B | ARG330 |
| B | TRP331 |
| B | TRP356 |
| B | ALA458 |
| B | HIS459 |
| B | HEC550 |
| B | HEM552 |
| B | HEM554 |
| site_id | BC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE HEM B 554 |
| Chain | Residue |
| B | LYS238 |
| B | ASP240 |
| B | THR244 |
| B | ARG245 |
| B | HIS279 |
| B | LEU282 |
| B | ASN306 |
| B | THR359 |
| B | CYS360 |
| B | CYS363 |
| B | HIS364 |
| B | PHE368 |
| B | TYR372 |
| B | HEM553 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 32 |
| 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 | 30 |
| 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 | 2 |
| 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 | 2 |
| 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 | CSA1 |
| Number of Residues | 5 |
| Details | a catalytic site defined by CSA, PubMed 9695195, 18336913 |
| Chain | Residue | Details |
| A | TYR467 | |
| A | HIS233 | |
| A | ASP267 | |
| A | TYR334 | |
| A | HIS268 |
| 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 |
