Structure of PDB 1aq8 Chain B

Receptor sequence
>1aq8B (length=331) Species: 511 (Alcaligenes faecalis) [Search protein sequence]
IAALPRQKVELVDPPFVHAHSQVAEGGPKVVEFTMVIEEKKIVIDDAGTE
VHAMAFNGTVPGPLMVVHQDDYLELTLINPETNTLMHNIDFHAATGALGG
GGLTEINPGEKTILRFKATKPGVFVYHCAPPGMVPWHVVSGMNGAIMVLP
REGLHDGKGKALTYDKIYYVGEQDFYVPRDENGKYKKYEAPGDAYEDTVK
VMRTLTPTHVVFNGAVGALTGDKAMTAAVGEKVLIVHSQANRDTRPHLIG
GHGDYVWATGKFNTPPDVDQETWFIPGGAAGAAFYTFQQPGIYAYVNHNL
IEAFELGAAAHFKVTGEWNDDLMTSVLAPSG
3D structure
PDB1aq8 Structure of nitrite bound to copper-containing nitrite reductase from Alcaligenes faecalis. Mechanistic implications.
ChainB
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H95 D98 H100 H135 C136 H145 M150 H255 E279 T280 H306
Catalytic site (residue number reindexed from 1) H87 D90 H92 H127 C128 H137 M142 H247 E271 T272 H298
Enzyme Commision number 1.7.2.1: nitrite reductase (NO-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 CU B H95 C136 H145 M150 H87 C128 H137 M142
BS02 CU B H100 H135 H92 H127
Gene Ontology
Molecular Function
GO:0005507 copper ion binding
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
GO:0050421 nitrite reductase (NO-forming) activity
Biological Process
GO:0019333 denitrification pathway
GO:0042128 nitrate assimilation
Cellular Component
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:1aq8, PDBe:1aq8, PDBj:1aq8
PDBsum1aq8
PubMed9353305
UniProtP38501|NIR_ALCFA Copper-containing nitrite reductase (Gene Name=nirK)

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