Structure of PDB 3sxq Chain B

Receptor sequence

>3sxqB (length=517) Species: 108010 (Thioalkalivibrio paradoxus) [Search protein sequence]

LKPVDALQCYDCHTQIEDMHVVGKHATVNCVHCHDATEHVETASARRMGE
RPVTHTSPEACASCHTAQFNSFASVRHESHPREEKANPRSRSPKFDTLIG
AHGFSLEHAEPRSHAFMLVDHFIVDRAYGGRFQYKSWQNVTDGLGAVRGA
WTVIEDMDPTTSDQRRFLAQTATAANPVCLNCKTQDHILDWAYMGDEHDA
AKWARTSKVVDFARDLHHPVNCYMCHDPHSTEPRVVRDALIHAVVDQGLG
TYPYDEAKSEHVTLTPVTFQRGGEDFRKIGLLNVADSNLMCGQCHVEYNC
NPGFQQSDGAPVGMDDRRTNHFFWANVFDYAEAAKEIDFFDFTHVTTGAP
LPKLQHPELETFWGSTHERNGVTCADCHMPRVKLENGKEYTMHSPRTPRD
MMNRACLNCHDGWTEAEAEYAIDYIKNYTHGKIMKAEFWLARMIDLFPVA
KRAGVSEDVLNEVRALHYDAHLHWEWWTAENSVGFHNPDQARESLMKSIT
KSKEGVGKLDAAIDAAV

3D structure

PDB

3sxq Comparative structural and functional analysis of two octaheme nitrite reductases from closely related Thioalkalivibrio species.

Chain

Resolution

1.9 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	B	A114 H126 V129 R131 C184 C187 K188 C299 H300 Y303 C305 F327 H361 N486	A109 H121 V124 R126 C179 C182 K183 C294 H295 Y298 C300 F322 H356 N481
BS02	HEC	B	H70 Q73 F77 C227 C230 H231 M295 Y395 T396 H398	H65 Q68 F72 C222 C225 H226 M290 Y390 T391 H393
BS03	HEC	B	S84 P116 R117 H119 F121 M122 D125 C187 M229 C296 C299 H300 P400	S79 P111 R112 H114 F116 M117 D120 C182 M224 C291 C294 H295 P395
BS04	HEC	B	H300 E363 F367 H372 T378 C379 C382 H383 T402 R404 I427 K431 N486 S487 F490 H491	H295 E358 F362 H367 T373 C374 C377 H378 T397 R399 I422 K426 N481 S482 F485 H486
BS05	HEC	B	T371 H372 P403 A410 C411 C414 H415 W418 F490	T366 H367 P398 A405 C406 C409 H410 W413 F485
BS06	HEC	B	H18 I21 H25 C35 C38 H39 T59 L194 Y228 P233 H234 R239 F274 R276 R282	H13 I16 H20 C30 C33 H34 T54 L189 Y223 P228 H229 R234 F269 R271 R277
BS07	HEC	B	K29 H30 V33 H37 C66 C69 H70 H231 T236	K24 H25 V28 H32 C61 C64 H65 H226 T231
BS08	HEC	B	C14 C17 H18 H39 A41 H44 V45 A48 S49 A50 M53 R56 P57 R276	C9 C12 H13 H34 A36 H39 V40 A43 S44 A45 M48 R51 P52 R271
BS09	CA	B	E302 Y303 K358 Q360	E297 Y298 K353 Q355
BS10	CO	B	H85 E88 E115	H80 E83 E110

Gene Ontology

	Molecular Function
GO:0016491	oxidoreductase activity
GO:0020037	heme binding
GO:0042279	nitrite reductase (cytochrome, ammonia-forming) activity
GO:0046872	metal ion binding

	Biological Process
GO:0019645	anaerobic electron transport chain

	Cellular Component
GO:0030288	outer membrane-bounded periplasmic space
GO:0042597	periplasmic space

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Molecular Function

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Biological Process

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Cellular Component

External links

PDB	RCSB:3sxq, PDBe:3sxq, PDBj:3sxq
PDBsum	3sxq
PubMed	22935005
UniProt	E7EDQ7

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