Structure of PDB 1oah Chain A

Receptor sequence

>1oahA (length=475) Species: 876 (Desulfovibrio desulfuricans) [Search protein sequence]

TGIAETETKMSAFKGQFPQQYASYMKNNEDRIMTDYKGSVPYHKNDNVNP
LPKGFKHAQPYLKNLWLGYPFMYEYNETRGHTYAIDDFLNIDRINRFAAD
GKGNLPATCWNCKTPKMMEWVSQYGDKFWSMDVNEFRAKDKINAHDETIG
CANCHDPATMELRLYSEPLKDWLKRSGKDWQKMSRNEKRTLVCAQCHVEY
YFTHKDNGPAAKPVFPWDNGFNPEDMYQYYKGHGAKGPDGKPGPFVDWVH
AASKVPMIKMQHPEYETFQDGPHGAAGVSCADCHMQYISSHWMTSPMKDP
EMRACRQCHADKTGEYLRQRVLYTQQKTFDQLLKAQEMSVKAHEAVRLAN
AYEGHRAANYEALMAEAREMVRKGQLFWDYVSAENSVGFHNPAKALDTLM
TSMECSQKAVDLATEATDFGIAPALAGDIKKLVPPILTLSRKLQQDPEFL
KQNPWTRLLPALPKAEQVWEGQDRA

3D structure

PDB

1oah Cytochrome C Nitrite Reductase from Desulfovibrio Desulfuricans Atcc 27774. The Relevance of the Two Calcium Sites in the Structure of the Catalytic Subunit (Nrfa)

Chain

Resolution

2.3 Å

3D
structure

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Enzymatic activity

Enzyme Commision number

1.7.2.2: nitrite reductase (cytochrome; ammonia-forming).

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	A	N113 T115 F125 I128 R130 C146 C149 K150 C233 H234 Y237 H299 N429	N76 T78 F88 I91 R93 C109 C112 K113 C196 H197 Y200 H262 N385
BS02	HEC	A	F54 Q57 Y61 G187 C188 C191 H192 R222 R226 M322 I332 S333 H335 M337	F17 Q20 Y24 G150 C151 C154 H155 R185 R189 M285 I288 S289 H291 M293
BS03	HEC	A	S76 T115 R116 H118 Y120 A121 D124 C149 K150 I186 Y202 C230 C233 H234 M337 T338	S39 T78 R79 H81 Y83 A84 D87 C112 K113 I149 Y165 C193 C196 H197 M293 T294
BS04	HEC	A	T71 K74 G75 H234 F305 H310 C317 C320 H321 S339 P340 M341 Q369 N429 F433 H434	T34 K37 G38 H197 F268 H273 C280 C283 H284 S295 P296 M297 Q325 N385 F389 H390
BS05	HEC	A	H310 V315 D319 C349 Q351 C352 H353 F433	H273 V278 D282 C305 Q307 C308 H309 F389
BS06	CA	A	E236 Y237 K296 Q298	E199 Y200 K259 Q261
BS07	CA	A	G75 E114 T115	G38 E77 T78
BS08	ZN	A	H399 D462	H355 D418
BS09	HEC	A	H353 K356	H309 K312

Gene Ontology

	Molecular Function
GO:0042279	nitrite reductase (cytochrome, ammonia-forming) activity

	Cellular Component
GO:0042597	periplasmic space

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Molecular Function

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Cellular Component

External links

PDB	RCSB:1oah, PDBe:1oah, PDBj:1oah
PDBsum	1oah
PubMed	12618432
UniProt	Q8VNU2

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