Structure of PDB 1r27 Chain C

Receptor sequence

>1r27C (length=1218) Species: 562 (Escherichia coli)

RDWEDGYRQRWQHDKIVRSTHGVNCTGSCSWKIYVKNGLVTWETQQTDYP
RTRPDLPNHEPRGCPRGASYSWYLYSANRLKYPMMRKRLMKMWREAKALH
SDPVEAWASIIEDADKAKSFKQARGRGGFVRSSWQEVNELIAASNVYTIK
NYGPDRVAGFSPIPAMSMVSYASGARYLSLIGGTCLSFYDWYCDLPPASP
QTWGEQTDVPESADWYNSSYIIAWGSNVPQTRTPDAHFFTEVRYKGTKTV
AVTPDYAEIAKLCDLWLAPKQGTDAAMALAMGHVMLREFHLDNPSQYFTD
YVRRYTDMPMLVMLEERDGYYAAGRMLRAADLVDALGQENNPEWKTVAFN
TNGEMVAPNGSIGFRWGEKGKWNLEQRDGKTGEETELQLSLLGSQDEIAE
VGFPYFGGDGTEHFNKVELENVLLHKLPVKRLQLADGSTALVTTVYDLTL
ANYGLERGLNDVNCATSYDDVKAYTPAWAEQITGVSRSQIIRIAREFADN
ADKTHGRSMIIVGAGLNHWYHLDMNYRGLINMLIFCGCVGQSGGGWAHYV
GQEKLRPQTGWQPLAFALDWQRPARHMNSTSYFYNHSSQWRYETVTAEEL
LSPMADKSRYTGHLIDFNVRAERMGWLPSAPQLGTNPLTIAGEAEKAGMN
PVDYTVKSLKEGSIRFAAEQPENGKNHPRNLFIWRSNLLGSSGKGHEFML
KYLLGTEHGIQGKDLGQQGGVKPEEVDWQDNGLEGKLDLVVTLDFRLSST
CLYSDIILPTATWYEKDDMNTSDMHPFIHPLSAAVDPAWEAKSDWEIYKA
IAKKFSEVCVGHLGKETDIVTLPIQHDSAAELAQPLDVKDWKKGECDLIP
GKTAPHIMVVERDYPATYERFTSIGPLMEKIGNGGKGIAWNTQSEMDLLR
KLNYTKAEGPAKGQPMLNTAIDAAEMILTLAPETNGQVAVKAWAALSEFT
GRDHTHLALNKEDEKIRFRDIQAQPRKIISSPTWSGLEDEHVSYNAGYTN
VHELIPWRTLSGRQQLYQDHQWMRDFGESLLVYRPPIDTRSVKEVIGQKS
NGNQEKALNFLTPHQKWGIHSTYSDNLLMLTLGRGGPVVWLSEADAKDLG
IADNDWIEVFNSNGALTARAVVSQRVPAGMTMMYHAQERIVNLPGSEITQ
QRGGIHNSVTRITPKPTHMIGGYAHLAYGFNYYGTVGSNRDEFVVVRKMK
NIDWLDGEGNDQVQESVK

3D structure

• PDB: 1r27 Architecture of NarGH reveals a structural classification of Mo-bisMGD enzymes
• Chain: C
• Resolution: 2.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R94 P190 W219 Y220 P224 Q580
• Catalytic site (residue number reindexed from 1): R66 P162 W191 Y192 P196 Q552
• Enzyme Commision number: 1.7.5.1: nitrate reductase (quinone).

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)	Binding affinity
BS01	MO	C	D222 G579	D194 G551
BS02	SF4	C	H49 V51 C53 G55 C57 W59 G91 C92 G95	H21 V23 C25 G27 C29 W31 G63 C64 G67
BS03	MGD	C	Y220 D222 H546 R713 S714 N715 S720 K722 L771 D772 F773 R774 T788 W791 K794 D822 T1090 H1092 H1098 S1099 T1100 H1163 N1185 N1217	Y192 D194 H518 R685 S686 N687 S692 K694 L743 D744 F745 R746 T760 W763 K766 D794 T1062 H1064 H1070 S1071 T1072 H1135 N1157 N1189
BS04	MGD	C	N52 R94 D222 G253 N255 Q258 T259 T281 P282 D283 Q299 D302 G541 A542 G543 L544 W547 V578 G579 P1091 H1092 Q1093 I1097 H1098 R1218	N24 R66 D194 G225 N227 Q230 T231 T253 P254 D255 Q271 D274 G513 A514 G515 L516 W519 V550 G551 P1063 H1064 Q1065 I1069 H1070 R1190

Gene Ontology

Molecular Function

• GO:0005515 protein binding
• GO:0008940 nitrate reductase activity
• GO:0009055 electron transfer activity
• GO:0016491 oxidoreductase activity
• GO:0043546 molybdopterin cofactor binding
• GO:0046872 metal ion binding
• GO:0051539 4 iron, 4 sulfur cluster binding
• GO:0160182 nitrate reductase (quinone) activity

Biological Process

• GO:0009061 anaerobic respiration
• GO:0019645 anaerobic electron transport chain
• GO:0042126 nitrate metabolic process
• GO:0042128 nitrate assimilation
• GO:0045333 cellular respiration

Cellular Component

• GO:0005886 plasma membrane
• GO:0009325 nitrate reductase complex
• GO:0016020 membrane
• GO:0044799 NarGHI complex
• GO:1990204 oxidoreductase complex

External links

• PDB: RCSB:1r27, PDBe:1r27, PDBj:1r27
• PDBsum: 1r27
• PubMed: 14725769
• UniProt: P09152|NARG_ECOLI Respiratory nitrate reductase 1 alpha chain (Gene Name=narG)