Structure of PDB 1ntd Chain A

Receptor sequence
>1ntdA (length=336) Species: 511 (Alcaligenes faecalis) [Search protein sequence]
TAAEIAALPRQKVELVDPPFVHAHSQVAEGGPKVVEFTMVIEEKKIVIDD
AGTEVHAMAFNGTVPGPLMVVHQDDYLELTLINPETNTLMHNIDFHAATG
ALGGGGLTEINPGEKTILRFKATKPGVFVYHCAPPGMVPWHVVSGENGAI
MVLPREGLHDGKGKALTYDKIYYVGEQDFYVPRDENGKYKKYEAPGDAYE
DTVKVMRTLTPTHVVFNGAVGALTGDKAMTAAVGEKVLIVHSQANRDTRP
HLIGGHGDYVWATGKFNTPPDVDQETWFIPGGAAGAAFYTFQQPGIYAYV
NHNLIEAFELGAAAHFKVTGEWNDDLMTSVLAPSGT
3D structure
PDB1ntd Structure of Alcaligenes faecalis nitrite reductase and a copper site mutant, M150E, that contains zinc.
ChainA
Resolution2.3 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 E150 H255 E279 T280 H306
Catalytic site (residue number reindexed from 1) H91 D94 H96 H131 C132 H141 E146 H251 E275 T276 H302
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 A H95 C136 H145 E150 H91 C132 H141 E146
BS02 CU A H100 H135 H96 H131
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:1ntd, PDBe:1ntd, PDBj:1ntd
PDBsum1ntd
PubMed7547950
UniProtP38501|NIR_ALCFA Copper-containing nitrite reductase (Gene Name=nirK)

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