Structure of PDB 2rdz Chain C

Receptor sequence

>2rdzC (length=441) Species: 562 (Escherichia coli) [Search protein sequence]

TVEAKNETFAPQHPDQYLSWKATSEQSERVDALAEDPRLVILWAGYPFSR
DYNKPRGHAFAVTDVRETLRTGAPKNAEDGPLPMACWSCKSPDVARLIQK
DGEDGYFHGKWARGGPEIVNNLGCADCHNTASPEFAKGKPELTLSRPYAA
RAMEAIGKPFEKAGRFDQQSMVCGQCHVEYYFDGKNKAVKFPWDDGMKVE
NMEQYYDKIAFSDWTNSLSKTPMLKAQHPEYETWTAGIHGKNNVTCIDCH
MPKVQNAEGKLYTDHKIGNPFDNFAQTCANCHTQDKAALQKVVAERKQSI
NDLKIKVEDQLVHAHFEAKAALDAGATEAEMKPIQDDIRHAQWRWDLAIA
SHGIHMHAPEEGLRMLGTAMDKAADARTKLARLLATKGITHEIQIPDIST
KEKAQQAIGLNMEQIKAEKQDFIKTVIPQWEEQARKNGLLS

3D structure

PDB

2rdz Role of a Conserved Glutamine Residue in Tuning the Catalytic Activity of Escherichia coli Cytochrome c Nitrite Reductase.

Chain

Resolution

1.74 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	CA	C	E215 Y216 K261 Q263	E179 Y180 K225 Q227
BS02	HEC	C	N89 P91 D100 T104 R106 C122 C125 K126 C212 H213 Y216 F218 H264 H388	N53 P55 D64 T68 R70 C86 C89 K90 C176 H177 Y180 F182 H228 H352
BS03	HEC	C	H49 Q52 W56 G159 C160 C163 H164 F171 G174 P176 L178 R201 Q205 I283 M287 Y298 T299 H301	H13 Q16 W20 G123 C124 C127 H128 F135 G138 P140 L142 R165 Q169 I247 M251 Y262 T263 H265
BS04	HEC	C	Q62 P91 R92 G93 H94 F96 A97 D100 C125 K126 L158 C209 C212 H213 H286 I303	Q26 P55 R56 G57 H58 F60 A61 D64 C89 K90 L122 C173 C176 H177 H250 I267
BS05	HEC	C	H213 E266 W270 H275 T281 C282 C285 H286 N305 P306 F307 H391 M392 H393	H177 E230 W234 H239 T245 C246 C249 H250 N269 P270 F271 H355 M356 H357
BS06	HEC	C	I274 H275 N278 V280 D284 C314 C317 H318 M392	I238 H239 N242 V244 D248 C278 C281 H282 M356
BS07	HEC	C	H318 Q320	H282 Q284

Gene Ontology

	Molecular Function
GO:0005506	iron ion binding
GO:0005509	calcium ion binding
GO:0016491	oxidoreductase activity
GO:0016966	nitric oxide reductase activity
GO:0020037	heme binding
GO:0042279	nitrite reductase (cytochrome, ammonia-forming) activity
GO:0046872	metal ion binding

	Biological Process
GO:0009061	anaerobic respiration
GO:0019645	anaerobic electron transport chain
GO:0042128	nitrate assimilation

	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:2rdz, PDBe:2rdz, PDBj:2rdz
PDBsum	2rdz
PubMed	18311941
UniProt	P0ABK9\|NRFA_ECOLI Cytochrome c-552 (Gene Name=nrfA)

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