Structure of PDB 4rwm Chain A

Receptor sequence
>4rwmA (length=497) Species: 174633 (Candidatus Kuenenia stuttgartiensis) [Search protein sequence]
GPTFQDVASQVFGQPVGPDNDGTLYIFGLTAKYTEPEYVDGRGPYKSFLK
MLPSIRWYDPEHYWTNGSQTEGVFKNEECVLCHTVQTPTIVNDWKQSSHG
SKDIRRGIGIKKDGKPVEDLVGCADCHGNNHQKLEMPTYKLCNDCHPKET
AEHRAGGLGSHTHAYTVNVLEFSWHVGKPAEEVTGCAHCHAIAENRCSGC
HTRHKFDPAEARKPTACRVCHMGIDHDEWAMYNTSIHGALYEAESARMDW
GKKLKKGNYRVPTCAYCHMQNGDHNPQRFGTIYSDMGMFQVDRGAPKHKA
KRDSWIKLCQDCHSPRFAADKLKEMDAGVNLSFTKWREAAAVIVGCYLDG
VVDPMPEGSAPDWYGHYTFSLLPGGDPRFYATSNLERLGLEMICYLTGNV
YKAYAHMSMYNQTYGNGSAFEQDRKLVEIKTEAAKLRRFAAIEKKIGLEH
KSADFWKHGEYLDLLPGWKRKPGDVDVEWFKRTDIPHRANADAGVEI
3D structure
PDB4rwm An unexpected reactivity of the P460 cofactor in hydroxylamine oxidoreductase.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H227 D262 H263 Y451
Catalytic site (residue number reindexed from 1) H190 D225 H226 Y414
Enzyme Commision number 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 EDO A W211 D262 M323 W174 D225 M286
BS02 EDO A L291 Y303 Q307 D348 L254 Y266 Q270 D311
BS03 EDO A Q314 G317 Q277 G280
BS04 EDO A I127 D130 R240 H241 I90 D93 R203 H204
BS05 EDO A G165 N166 N167 K170 G128 N129 N130 K133
BS06 HG1 A L408 L409 P410 G411 L371 L372 P373 G374
BS07 HEC A W101 S105 Q106 T107 F111 C116 C119 H120 Q123 C160 A161 G165 N166 H168 L171 W64 S68 Q69 T70 F74 C79 C82 H83 Q86 C123 A124 G128 N129 H131 L134
BS08 HEC A H120 I127 H136 G159 C160 C163 H164 M173 P174 R233 S235 R240 H241 H83 I90 H99 G122 C123 C126 H127 M136 P137 R196 S198 R203 H204
BS09 HEC A S135 H136 R142 R143 G144 I145 I147 C179 C182 H183 F243 P245 S98 H99 R105 R106 G107 I108 I110 C142 C145 H146 F206 P208
BS10 HEC A N205 F209 H212 C223 C226 H227 C257 H258 H263 Y320 D322 M323 K439 R525 N168 F172 H175 C186 C189 H190 C220 H221 H226 Y283 D285 M286 K402 R488
BS11 HEC A R143 H183 E186 H190 C234 C237 H238 A248 R249 L291 M306 G309 H311 R106 H146 E149 H153 C197 C200 H201 A211 R212 L254 M269 G272 H274
BS12 HEC A G196 S197 H198 A201 N205 C226 H227 I229 G236 C237 A253 C254 C257 H258 C301 Q314 Y320 G159 S160 H161 A164 N168 C189 H190 I192 G199 C200 A216 C217 C220 H221 C264 Q277 Y283
BS13 HEC A H258 E265 Y269 P299 T300 C301 C304 H305 T318 W342 Y438 A442 H443 H221 E228 Y232 P262 T263 C264 C267 H268 T281 W305 Y401 A405 H406
BS14 HEC A I273 H274 L277 R297 P299 C346 C349 H350 F354 K358 M444 I236 H237 L240 R260 P262 C309 C312 H313 F317 K321 M407
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
Biological Process
GO:0006809 nitric oxide biosynthetic 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:4rwm, PDBe:4rwm, PDBj:4rwm
PDBsum4rwm
PubMed26249351
UniProtQ1PX48|HAO_KUEST Hydroxylamine oxidoreductase (Gene Name=hao)

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