Structure of PDB 4n4o Chain E

Receptor sequence
>4n4oE (length=503) Species: 915 (Nitrosomonas europaea) [Search protein sequence]
DISTVPDETYDALKLDRGKATPKETYEALVKRYKDPAHGAGKGTMGDYWE
PIAISIYMDPNTFYKPPVSPKEVAERKDCVECHSDETPVWVRAWKRSTHA
NLDKIRNLKSDDPLYYKKGKLEEVENNLRSMGKLGEKETLKEVGCIDCHV
DVNKKDKADHTKDIRMPTADTCGTCHLREFAERESERDTMVWPNGQWPAG
RPSHALDYTANIETTVWAAMPQREVAEGCTMCHTNQNKCDNCHTRHEFSA
AESRKPEACATCHSGVDHNNWEAYTMSKHGKLAEMNRDKWNWEVRLKDAF
SKGGQNAPTCAACHMEYEGEYTHNITRKTRWANYPFVPGIAENITSDWSE
ARLDSWVLTCTQCHSERFARSYLDLMDKGTLEGLAKYQEANAIVHKMYED
GTLTGQKTNRPNPPEPEKPGFGIFTQLFWSKGNNPASLELKVLEMAENNL
AKMHVGLAHVNPGGWTYTEGWGPMNRAYVEIQDEYTKMQELSALQARVNK
LEG
3D structure
PDB4n4o Structural Basis of Biological NO Generation by Octaheme Oxidoreductases.
ChainE
Resolution2.472 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H257 D291 H292 Y358 Y491
Catalytic site (residue number reindexed from 1) H233 D267 H268 Y334 Y467
Enzyme Commision number 1.7.2.6: hydroxylamine dehydrogenase.
1.7.2.9: hydroxylamine oxidase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 HEC E W114 K262 D264 T268 R269 W90 K238 D240 T244 R245
BS02 HEC E W221 R225 A234 N235 T238 C253 C256 H257 H287 H292 N357 F452 W197 R201 A210 N211 T214 C229 C232 H233 H263 H268 N333 F428
BS03 HEC E E390 R391 E366 R367
BS04 HEC E H388 S389 H364 S365
BS05 HEC E Y140 K141 H200 E203 C263 C266 H267 A274 S277 R278 R319 L320 M339 H347 Y116 K117 H176 E179 C239 C242 H243 A250 S253 R254 R295 L296 M315 H323
BS06 HEC E T122 H123 K141 K144 L145 V167 C196 C199 H200 C263 H267 F272 S273 A274 T98 H99 K117 K120 L121 V143 C172 C175 H176 C239 H243 F248 S249 A250
BS07 HEC E Y81 Y88 P94 E96 A98 C103 C106 H107 E110 C169 H173 H184 I188 Y57 Y64 P70 E72 A74 C79 C82 H83 E86 C145 H149 H160 I164
BS08 HEC E Y81 H107 W114 W118 H123 G168 C169 C172 H173 M190 P191 D264 R269 H270 F272 Y57 H83 W90 W94 H99 G144 C145 C148 H149 M166 P167 D240 R245 H246 F248
BS09 HEC E H287 N294 Y298 P332 T333 C334 C337 H338 T353 R354 W355 W380 M400 A482 H483 H263 N270 Y274 P308 T309 C310 C313 H314 T329 R330 W331 W356 M376 A458 H459
BS10 HEC E P226 S227 H228 D231 A234 C256 H257 N259 N265 C266 C283 C286 H287 C334 I349 T353 A356 P202 S203 H204 D207 A210 C232 H233 N235 N241 C242 C259 C262 H263 C310 I325 T329 A332
BS11 HEC E H303 L306 F324 N330 A331 P332 C384 C387 H388 F392 Y396 V484 H279 L282 F300 N306 A307 P308 C360 C363 H364 F368 Y372 V460
BS12 HOA E D291 H292 D267 H268
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0020037 heme binding
GO:0033740 hydroxylamine oxidoreductase activity
GO:0042802 identical protein binding
GO:0046872 metal ion binding
GO:0047991 hydroxylamine oxidase activity
Biological Process
GO:0019331 anaerobic respiration, using ammonium as electron donor
GO:0070207 protein homotrimerization
Cellular Component
GO:0044222 anammoxosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4n4o, PDBe:4n4o, PDBj:4n4o
PDBsum4n4o
PubMed24302732
UniProtQ50925|HAO_NITEU Hydroxylamine oxidoreductase (Gene Name=hao1)

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