Structure of PDB 6tfd Chain B

Receptor sequence

>6tfdB (length=423) Species: 670307 (Hyphomicrobium denitrificans 1NES1)

SHAPVVFTLRTGIAEGRMVYIGVGGDIDRQVNPKLVVHEGETVQINLING
EGAQHDAVIDQYAARSAIVSGKNASSTFSFIASKVGQFDYYCSLPGHRQA
GMQGVLQVVPGNRAEMPSTAADITRDPADLPGPIGARQAKTVRIDLETVE
LKGQLDDKTTYTYWTFNGKVPGPFLRVRVGDTVELHLKNAKDSLMIHSVD
FHGATGPGGAAAYTQTDPGAETVVTFKALVPGIFVYHCATPSVPNHITNG
MYGLLLVEPEGGLPQVDREFYVMQGEIYTVKPFGTSGEQEMDYEKLISEK
PEYFLFNGSVGALTRTHPLYANVGETVRIFFGVGGPNFTSSFHVIGEIFD
HVYALGSVTSPPLTGVQTVSVPPGGATIVDFKLDRGGRYVLVDHALSRLD
HGLVGFLNVDGPKNDAIMHEGPP

3D structure

• PDB: 6tfd 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.
• Chain: B
• Resolution: 2.25 Å

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	B	D225 H227 H262	D200 H202 H237
BS02	CU	B	H222 C263 H271 M276	H197 C238 H246 M251
BS03	CU	B	H227 H262	H202 H237
BS04	CU	B	H80 C117 H122	H55 C92 H97
BS05	NO	B	H368 I370 H419	H343 I345 H394

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

External links

• PDB: RCSB:6tfd, PDBe:6tfd, PDBj:6tfd
• PDBsum: 6tfd
• PubMed: 32431838
• UniProt: N0B9M5