Structure of PDB 4fas Chain B

Receptor sequence

>4fasB (length=502) Species: 228410 (Nitrosomonas europaea ATCC 19718) [Search protein sequence]

DISTVPDETYDALKLDRGKATPKETYEALVKRYKDPAHGAGKGTMGDYWE
PIAISIYMDPNTFYKPPVSPKEVAERKDCVECHSDETPVWVRAWKRSTHA
NLDKIRNLKSDDPLYYKKGKLEEVENNLRSMGKLGEKETLKEVGCIDCHV
DVNKKDKADHTKDIRMPTADTCGTCHLREFAERESERDTMVWPNGQWPAG
RPSHALDYTANIETTVWAAMPQREVAEGCTMCHTNQNKCDNCHTRHEFSA
AESRKPEACATCHSGVDHNNWEAYTMSKHGKLAEMNRDKWNWEVRLKDAF
SKGGQNAPTCAACHMEYEGEYTHNITRKTRWANYPFVPGIAENITSDWSE
ARLDSWVLTCTQCHSERFARSYLDLMDKGTLEGLAKYQEANAIVHKMYED
GTLTGQKTNRPNPPEPEKPGFGIFTQLFWSKGNNPASLELKVLEMAENNL
AKMHVGLAHVNPGGWTYTEGWGPMNRAYVEIQDEYTKMQELSALQARVNK
LE

3D structure

PDB

4fas Structural studies of hydroxylamine oxidoreductase reveal a unique heme cofactor and a previously unidentified interaction partner.

Chain

Resolution

2.1 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	H233 D267 H268 Y334 Y467
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)
BS01	HEC	B	W90 K238 D240 T244 R245	W90 K238 D240 T244 R245
BS02	ISW	B	W197 R201 A210 N211 T214 W217 C229 C232 H233 C262 H263 H268 N333 F428	W197 R201 A210 N211 T214 W217 C229 C232 H233 C262 H263 H268 N333 F428
BS03	HEC	B	Y57 Y64 P70 A74 D78 C79 C82 H83 E86 C145 H149 H160 I164	Y57 Y64 P70 A74 D78 C79 C82 H83 E86 C145 H149 H160 I164
BS04	HEC	B	Y57 H83 W90 H99 G144 C145 C148 H149 M166 P167 K238 D240 R245 H246 F248	Y57 H83 W90 H99 G144 C145 C148 H149 M166 P167 K238 D240 R245 H246 F248
BS05	HEC	B	T98 H99 K117 K120 L121 V124 V143 C172 C175 H176 C239 H243 F248 A250	T98 H99 K117 K120 L121 V124 V143 C172 C175 H176 C239 H243 F248 A250
BS06	HEC	B	Y116 K117 H176 E179 H204 C239 C242 H243 S253 R254 R295 L296 M315 H323	Y116 K117 H176 E179 H204 C239 C242 H243 S253 R254 R295 L296 M315 H323
BS07	HEC	B	P202 S203 H204 D207 C232 H233 N235 N241 C242 C259 C262 H263 C310 I325 A332	P202 S203 H204 D207 C232 H233 N235 N241 C242 C259 C262 H263 C310 I325 A332
BS08	HEC	B	H263 N270 Y274 P308 T309 C310 C313 H314 T329 R330 W331 W356 A458 H459	H263 N270 Y274 P308 T309 C310 C313 H314 T329 R330 W331 W356 A458 H459
BS09	HEC	B	H279 F300 N306 A307 P308 C360 C363 H364 F368 Y372 V460	H279 F300 N306 A307 P308 C360 C363 H364 F368 Y372 V460
BS10	ISW	B	G463 Y467	G463 Y467
BS11	HEC	B	S365 E366 R367	S365 E366 R367
BS12	HEC	B	H364 S365	H364 S365

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:4fas, PDBe:4fas, PDBj:4fas
PDBsum	4fas
PubMed	23952581
UniProt	Q50925\|HAO_NITEU Hydroxylamine oxidoreductase (Gene Name=hao1)

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