Structure of PDB 6zau Chain A

Receptor sequence

>6zauA (length=345) Species: 566679 (Bradyrhizobium sp. ORS 375)

DLKLPRQRVDLVAPPFVHVHEQATKQGPKIMEFKLVVQEKKMVIDEKGTT
FQAMTFNGSMPGPLMVVHEGDYVEVTLVNPATNTMPHNIDFHSATGALGG
GALTLINPGEQVVLRWKATRTGVFVYHCAPGGPMIPWHVVSGMNGAVMVL
PRDGLNDGHGHSLRYDRIYYIGEQDLYVPRDEKGNFKSYDSPGEAYSDTE
EVMRKLTPTHVVFNGKAGALTGKNALNANVGENVLIVHSQANRDSRPHLI
GGHGDYVWETGKFSNAPETGLETWFIRGGSAGAALYKFLQPGIYAYVTHN
LIEAANLGATAHFKVEGKWNDDLMTQVKAPADIPTGSTNENLYFQ

3D structure

• PDB: 6zau An unprecedented insight into the catalytic mechanism of copper nitrite reductase from atomic-resolution and damage-free structures.
• Chain: A
• Resolution: 1.3 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H89 D92 H94 H129 C130 H140 M145 H250 E274 T275 H301
• Catalytic site (residue number reindexed from 1): H87 D90 H92 H127 C128 H138 M143 H248 E272 T273 H299
• 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	GLC	A	K49 R182 G186	K47 R180 G184
BS02	FRU	A	K185 G186 N187	K183 G184 N185
BS03	CU	A	H89 C130 H140 M145	H87 C128 H138 M143
BS04	CU	A	H94 H129	H92 H127
BS05	NO	A	K43 T52 S190 Y191	K41 T50 S188 Y189
BS06	NO	A	M136 H140	M134 H138
BS07	NO2	A	D92 H94 H129	D90 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

External links

• PDB: RCSB:6zau, PDBe:6zau, PDBj:6zau
• PDBsum: 6zau
• PubMed: 33523860
• UniProt: H0SLX7