Structure of PDB 1ogy Chain E

Receptor sequence

>1ogyE (length=789) Species: 1063 (Cereibacter sphaeroides) [Search protein sequence]

IRWSKAPCRFCGTGCGVMVGTRDGQVVATHGDTQAEVNRGLNCVKGYFLS
KIMYGEDRLTTPLLRMKDGVYHKEGEFAPVSWDEAFDVMAAQAKLVLKEK
APEAVGMFGSGQWTIWEGYAASKLMRAGFRSNNLDPNARHCMASAATAFM
RTFGMDEPMGCYDDFEAADAFVLWGSNMAEMHPILWSRLTDRRLSHEHVR
VAVLSTFTHRSSDLSDTPIIFRPGTDRAILNYIAHHIISTGRVNRDFVDR
HTNFALGATDIGYGLRPEHQLQLAAKGAADAGAMTPTDFETFAALVSEYT
LEKAAEISGVEPALLEELAELYADPDRKWMSLWTMGFNQHVRGVWANHMV
YNLHLLTGKISEPGNSPFSLTGQPFACGTAREVGTFAHRLPADMVVTNPE
HRAHAEEIWKLPAGLLPDWVGAHAVEQDRKLHDGEINFYWVQVNNNMQAA
PNIDQETYPGYRNPENFIVVSDAYPTVTGRAADLVLPAAMWVEKEGAYGN
AERRTHFWHQLVEAPGEARSDLWQLMEFSKRFTTDEVWPEEILSAAPAYR
GKTLFEVLFANGSVDRFPASDVNPDHANHEAALFGFYPQKGLFEEYAAFG
RGHGHDLAPFDTYHEVRGLHWPVVEGEETRWRYREGFDPYVKPGEGLRFY
GKPDGRAVILGVPYEPPAESPDEEFGFWLVTGRVLEHWHSGSMTLRWPEL
YKAFPGAVCFMHPEDARSRGLNRGSEVRVISRRGEIRTRLETRGRNRMPR
GVVFVPWFDASQLINKVTLDANDPISRQTDFKKCAVKIE

3D structure

PDB

1ogy Structural and Redox Plasticity in the Heterodimeric Periplasmic Nitrate Reductase

Chain

Resolution

3.2 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	N53 C54 K56 G122 W124 C152 M153 M346 T382 G383 Q384
Catalytic site (residue number reindexed from 1)	N42 C43 K45 G111 W113 C141 M142 M335 T371 G372 Q373
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	E	C19 C22 C26 N53 C54 I195	C8 C11 C15 N42 C43 I184
BS02	MGD	E	R20 Q123 N148 H151 C152 Q350 Q384 V454 N455 N456 A460 S482 D483 A499 M501 D532 T692 R694 W699 H700 S701 S703 W768 N776 F792	R9 Q112 N137 H140 C141 Q339 Q373 V443 N444 N445 A449 S471 D472 A488 M490 D521 T681 R683 W688 H689 S690 S692 W757 N765 F781
BS03	MGD	E	K56 G186 N188 M192 S216 T217 H220 F232 G235 D237 T345 M346 G347 F348 G383 Q384 G693 R694 V695 L696 H698 W699 H700 K793 K794	K45 G175 N177 M181 S205 T206 H209 F221 G224 D226 T334 M335 G336 F337 G372 Q373 G682 R683 V684 L685 H687 W688 H689 K782 K783

Gene Ontology

	Molecular Function
GO:0005506	iron ion 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:0042128	nitrate assimilation
GO:0045333	cellular respiration

	Cellular Component
GO:0042597	periplasmic space
GO:1990204	oxidoreductase complex

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Molecular Function

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Biological Process

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Cellular Component

External links

PDB	RCSB:1ogy, PDBe:1ogy, PDBj:1ogy
PDBsum	1ogy
PubMed	14528294
UniProt	Q53176\|NAPA_CERS4 Periplasmic nitrate reductase (Gene Name=napA)

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