Structure of PDB 6tfd Chain C

Receptor sequence
>6tfdC (length=423) Species: 670307 (Hyphomicrobium denitrificans 1NES1) [Search protein sequence]
SHAPVVFTLRTGIAEGRMVYIGVGGDIDRQVNPKLVVHEGETVQINLING
EGAQHDAVIDQYAARSAIVSGKNASSTFSFIASKVGQFDYYCSLPGHRQA
GMQGVLQVVPGNRAEMPSTAADITRDPADLPGPIGARQAKTVRIDLETVE
LKGQLDDKTTYTYWTFNGKVPGPFLRVRVGDTVELHLKNAKDSLMIHSVD
FHGATGPGGAAAYTQTDPGAETVVTFKALVPGIFVYHCATPSVPNHITNG
MYGLLLVEPEGGLPQVDREFYVMQGEIYTVKPFGTSGEQEMDYEKLISEK
PEYFLFNGSVGALTRTHPLYANVGETVRIFFGVGGPNFTSSFHVIGEIFD
HVYALGSVTSPPLTGVQTVSVPPGGATIVDFKLDRGGRYVLVDHALSRLD
HGLVGFLNVDGPKNDAIMHEGPP
3D structure
PDB6tfd Structures of substrate- and product-bound forms of a multi-domain copper nitrite reductase shed light on the role of domain tethering in protein complexes.
ChainC
Resolution2.25 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H222 D225 H227 H262 C263 H271 M276 H368 Q392 T393 H419
Catalytic site (residue number reindexed from 1) H197 D200 H202 H237 C238 H246 M251 H343 Q367 T368 H394
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 NO2 C H368 I370 H419 H343 I345 H394
BS02 CU C H222 C263 H271 M276 H197 C238 H246 M251
BS03 CU C H227 H262 H202 H237
BS04 CU C H80 C117 H122 H55 C92 H97
Gene Ontology
Molecular Function
GO:0005507 copper ion binding
GO:0009055 electron transfer activity
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
GO:0050421 nitrite reductase (NO-forming) activity

View graph for
Molecular Function
External links
PDB RCSB:6tfd, PDBe:6tfd, PDBj:6tfd
PDBsum6tfd
PubMed32431838
UniProtN0B9M5

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