Structure of PDB 2j7a Chain H

Receptor sequence

>2j7aH (length=497) Species: 882 (Nitratidesulfovibrio vulgaris str. Hildenborough)

GCSDVSTELKTPVYKTKLTAEEIRNSAFKPEFPKQYASYERNDETTVMTE
YKGSVPFNKNDNVNPLPEGYRHAQPYLKNLWLGYPFMYEYREARGHTYAI
QDFLHIDRINRYAEKGGLPATCWNCKTPKMMEWVKESGDGFWAKDVNEFR
DKIDMKDHTIGCATCHDPQTMELRITSVPLTDYLVSQGKDPKKLPRNEMR
ALVCGQCHVEYYFNGPTMGVNKKPVFPWAEGFDPADMYRYYDKHGDLQVK
GFEGKFADWTHPASKTPMIKAQHPEYETWINGTHGAAGVTCADCHMSYTR
SDDKKKISSHWWTSPMKDPEMRACRQCHSDKTPDYLKSRVLFTQKRTFDL
LLAAQEVSVKAHEAVRLANEYQGAKAAGYDDLMIQAREMVRKGQFFWDYV
SAENSVGFHNPAKALDTLAQSQQFSQKAIDLAMEATQYGIGKDLSGDIKT
IVPPILKMNRKLQQDPEFMKTHKWFQYLPVLPKADQVWDGQKRLVSA

3D structure

• PDB: 2j7a X-Ray Structure of the Membrane-Bound Cytochrome C Quinol Dehydrogenase Nrfh Reveals Novel Haem Coordination.
• Chain: H
• Resolution: 2.3 Å

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)	Binding affinity
BS01	HEC	H	H353 K356	H328 K331
BS02	HEC	H	R116 A118 F128 I131 R133 C147 C150 K151 C232 H233 Y236 H298 N429	R91 A93 F103 I106 R108 C122 C125 K126 C207 H208 Y211 H273 N404
BS03	HEC	H	Y39 F57 Q60 Y64 G186 C187 C190 H191 M196 L198 R221 R225 M321 I332 S333 H335 W337	Y14 F32 Q35 Y39 G161 C162 C165 H166 M171 L173 R196 R200 M296 I307 S308 H310 W312
BS04	HEC	H	S79 A118 R119 H121 Y123 A124 D127 C150 K151 I185 T189 C229 C232 H233 H320 W337 T338	S54 A93 R94 H96 Y98 A99 D102 C125 K126 I160 T164 C204 C207 H208 H295 W312 T313
BS05	HEC	H	T74 K77 H233 E300 W304 H309 T315 C316 C319 H320 S339 P340 M341 Q369 N429 S430 F433 H434	T49 K52 H208 E275 W279 H284 T290 C291 C294 H295 S314 P315 M316 Q344 N404 S405 F408 H409
BS06	HEC	H	H309 V314 C319 C349 C352 H353 F433	H284 V289 C294 C324 C327 H328 F408
BS07	CA	H	E235 Y236 K295 Q297	E210 Y211 K270 Q272
BS08	CA	H	G78 E117 A118	G53 E92 A93

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:0005886 plasma membrane
• GO:0030288 outer membrane-bounded periplasmic space
• GO:0042597 periplasmic space

External links

• PDB: RCSB:2j7a, PDBe:2j7a, PDBj:2j7a
• PDBsum: 2j7a
• PubMed: 17139260
• UniProt: Q72EF3|NRFA_NITV2 Cytochrome c nitrite reductase subunit NrfA (Gene Name=nrfA)