Structure of PDB 3h4h Chain B

Receptor sequence
>3h4hB (length=335) Species: 511 (Alcaligenes faecalis) [Search protein sequence]
TAAEIAALPRQKVELVDPPFVHAHSQVAEGGPKVVEFTMVIEEKKIVIDD
AGTEVHAMAFNGTVPGPLMVVHQDDYLELTLINPETNTLTHNIDFHAATG
ALGGGGLTEINPGEKTILRFKATKPGVFVYHCAPPGMVPWHVVSGMNGAI
MVLPREGLHDGKGKALTYDKIYYVGEQDFYVPRDENGKYKKYEAPGDAYE
DTVKVMRTLTPTHVVFNGAVGALTGDKAMTAAVGEKVLIVHSQANRDTRP
HLIGGHGDYVWATGKFNTPPDVDQETWFIPGGAAGAAFYTFQQPGIYAYV
NHNLIEACELGAAAHFKVTGEWNDDLMTSVLAPSG
3D structure
PDB3h4h Directed evolution of copper nitrite reductase to a chromogenic reductant.
ChainB
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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) H91 D94 H96 H131 C132 H141 M146 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 B H95 C136 H145 M150 H91 C132 H141 M146
BS02 CU B 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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3h4h, PDBe:3h4h, PDBj:3h4h
PDBsum3h4h
PubMed20083495
UniProtP38501|NIR_ALCFA Copper-containing nitrite reductase (Gene Name=nirK)

[Back to BioLiP]