Structure of PDB 4n4l Chain A

Receptor sequence

>4n4lA (length=497) Species: 174633 (Candidatus Kuenenia stuttgartiensis) [Search protein sequence]

GPTFQDVASQVFGQPVGPDNDGTLYIFGLTAKYTEPEYVDGRGPYKSFLK
MLPSIRWYDPEHYWTNGSQTEGVFKNEECVLCHTVQTPTIVNDWKQSSHG
SKDIRRGIGIKKDGKPVEDLVGCADCHGNNHQKLEMPTYKLCNDCHPKET
AEHRAGGLGSHTHAYTVNVLEFSWHVGKPAEEVTGCAHCHAIAENRCSGC
HTRHKFDPAEARKPTACRVCHMGIDHDEWAMYNTSIHGALYEAESARMDW
GKKLKKGNYRVPTCAYCHMQNGDHNPQRFGTIYSDMGMFQVDRGAPKHKA
KRDSWIKLCQDCHSPRFAADKLKEMDAGVNLSFTKWREAAAVIVGCYLDG
VVDPMPEGSAPDWYGHYTFSLLPGGDPRFYATSNLERLGLEMICYLTGNV
YKAYAHMSMYNQTYGNGSAFEQDRKLVEIKTEAAKLRRFAAIEKKIGLEH
KSADFWKHGEYLDLLPGWKRKPGDVDVEWFKRTDIPHRANADAGVEI

3D structure

PDB

4n4l Structural Basis of Biological NO Generation by Octaheme Oxidoreductases.

Chain

Resolution

1.9 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)
BS01	HZN	A	D262 H263	D225 H226
BS02	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
BS03	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
BS04	HEC	A	S135 H136 R142 R143 G144 I145 I147 V154 C179 C182 H183 F243 P245	S98 H99 R105 R106 G107 I108 I110 V117 C142 C145 H146 F206 P208
BS05	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
BS06	HEC	A	R143 H183 E186 H190 C234 C237 H238 A248 R249 K290 L291 M306 G309 H311	R106 H146 E149 H153 C197 C200 H201 A211 R212 K253 L254 M269 G272 H274
BS07	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
BS08	HEC	A	H258 E265 Y269 P299 T300 C301 C304 H305 T318 R330 W342 Y438 A442 H443	H221 E228 Y232 P262 T263 C264 C267 H268 T281 R293 W305 Y401 A405 H406
BS09	HEC	A	I273 H274 L277 R297 P299 C346 C349 H350 F354 K358 M444	I236 H237 L240 R260 P262 C309 C312 H313 F317 K321 M407
BS10	HG1	A	L408 L409 P410 G411	L371 L372 P373 G374

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:4n4l, PDBe:4n4l, PDBj:4n4l
PDBsum	4n4l
PubMed	24302732
UniProt	Q1PX48\|HAO_KUEST Hydroxylamine oxidoreductase (Gene Name=hao)

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