Structure of PDB 2nya Chain A

Receptor sequence

>2nyaA (length=791) Species: 83333 (Escherichia coli K-12) [Search protein sequence]

EAIKWDKAPCRFCGTGCGVLVGTQQGRVVACQGDPDAPVNRGLNCIKGYF
LPKIMYGKDRLTQPLLRMKNGKYDKEGEFTPITWDQAFDVMEEKFKTALK
EKGPESIGMFGSGQWTIWEGYAASKLFKAGFRSNNIDPNARHCMASAVVG
FMRTFGMDEPMGCYDDIEQADAFVLWGANMAEMHPILWSRITNRRLSNQN
VTVAVLSTYQHRSFELADNGIIFTPQSDLVILNYIANYIIQNNAINQDFF
SKHVNLRKGATDIGYGLRPTHPLEKAAKNPGSDASEPMSFEDYKAFVAEY
TLEKTAEMTGVPKDQLEQLAQLYADPNKKVISYWTMGFNQHTRGVWANNL
VYNLHLLTGKISQPGCGPFSLTGQPSACGTAREVGTFAHRLPADMVVTNE
KHRDICEKKWNIPSGTIPAKIGLHAVAQDRALKDGKLNVYWTMCTNNMQA
GPNINEERMPGWRDPRNFIIVSDPYPTVSALAADLILPTAMWVEKEGAYG
NAERRTQFWRQQVQAPGEAKSDLWQLVQFSRRFKTEEVWPEDLLAKKPEL
RGKTLYEVLYATPEVSKFPVSELAEDQLNDESRELGFYLQKGLFEEYAWF
GRGHGHDLAPFDDYHKARGLRWPVVNGKETQWRYSEGNDPYVKAGEGYKF
YGKPDGKAVIFALPFEPAAEAPDEEYDLWLSTGRVLEHWHTGSMTRRVPE
LHRAFPEAVLFIHPLDAKARDLRRGDKVKVVSRRGEVISIVETRGRNRPP
QGLVYMPFFDAAQLVNKLTLDATDPLSKETDFKKCAVKLEK

3D structure

PDB

2nya Spectropotentiometric and structural analysis of the periplasmic nitrate reductase from Escherichia coli

Chain

Resolution

2.5 Å

3D
structure

Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]

Enzymatic activity

Catalytic site (original residue number in PDB)	N44 C45 K47 C143 M144 M183 M336 T372 G373 Q374
Catalytic site (residue number reindexed from 1)	N44 C45 K47 C143 M144 M183 M336 T372 G373 Q374
Enzyme Commision number	1.9.6.1: nitrate reductase (cytochrome).

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	SF4	A	C10 C13 C17 C45 I186	C10 C13 C17 C45 I186
BS02	MGD	A	R11 Q114 N139 C143 M336 Q340 Q374 C444 T445 N446 A450 S472 D473 P474 T489 A490 M491 K495 D522 T682 R684 H690 T691 S693 F758 N766 F782	R11 Q114 N139 C143 M336 Q340 Q374 C444 T445 N446 A450 S472 D473 P474 T489 A490 M491 K495 D522 T682 R684 H690 T691 S693 F758 N766 F782
BS03	MGD	A	K47 W176 G177 M183 S207 T208 Y209 F223 D228 T335 M336 G337 F338 G373 Q374 G683 R684 L686 H688 W689 H690 K783 K784	K47 W176 G177 M183 S207 T208 Y209 F223 D228 T335 M336 G337 F338 G373 Q374 G683 R684 L686 H688 W689 H690 K783 K784

Gene Ontology

	Molecular Function
GO:0005506	iron ion binding
GO:0005515	protein binding
GO:0008940	nitrate reductase activity
GO:0009055	electron transfer activity
GO:0016491	oxidoreductase activity
GO:0030151	molybdenum ion binding
GO:0043546	molybdopterin cofactor binding
GO:0046872	metal ion binding
GO:0050140	nitrate reductase (cytochrome) activity
GO:0051539	4 iron, 4 sulfur cluster binding

	Biological Process
GO:0006777	Mo-molybdopterin cofactor biosynthetic process
GO:0009061	anaerobic respiration
GO:0042128	nitrate assimilation
GO:0045333	cellular respiration

	Cellular Component
GO:0009325	nitrate reductase complex
GO:0030288	outer membrane-bounded periplasmic space
GO:0042597	periplasmic space
GO:1990204	oxidoreductase complex

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component

External links

PDB	RCSB:2nya, PDBe:2nya, PDBj:2nya
PDBsum	2nya
PubMed	17130127
UniProt	P33937\|NAPA_ECOLI Periplasmic nitrate reductase (Gene Name=napA)

[Back to BioLiP]