Structure of PDB 6zaw Chain A Binding Site BS03

Receptor Information
>6zaw Chain A (length=345) Species: 566679 (Bradyrhizobium sp. ORS 375) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DLKLPRQRVDLVAPPFVHVHEQATKQGPKIMEFKLVVQEKKMVIDEKGTT
FQAMTFNGSMPGPLMVVHEGDYVEVTLVNPATNTMPHNIDFHSATGALGG
GALTLINPGEQVVLRWKATRTGVFVYHCAPGGPMIPWHVVSGMNGAVMVL
PRDGLNDGHGHSLRYDRIYYIGEQDLYVPRDEKGNFKSYDSPGEAYSDTE
EVMRKLTPTHVVFNGKAGALTGKNALNANVGENVLIVHSQANRDSRPHLI
GGHGDYVWETGKFSNAPETGLETWFIRGGSAGAALYKFLQPGIYAYVTHN
LIEAANLGATAHFKVEGKWNDDLMTQVKAPADIPTGSTNENLYFQ
Ligand information
Ligand IDFRU
InChIInChI=1S/C6H12O6/c7-1-3-4(9)5(10)6(11,2-8)12-3/h3-5,7-11H,1-2H2/t3-,4-,5+,6-/m1/s1
InChIKeyRFSUNEUAIZKAJO-ARQDHWQXSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04OC1C(O)C(OC1(O)CO)CO
OpenEye OEToolkits 1.5.0C([C@@H]1[C@H]([C@@H]([C@](O1)(CO)O)O)O)O
CACTVS 3.341OC[CH]1O[C](O)(CO)[CH](O)[CH]1O
OpenEye OEToolkits 1.5.0C(C1C(C(C(O1)(CO)O)O)O)O
CACTVS 3.341OC[C@H]1O[C@](O)(CO)[C@@H](O)[C@@H]1O
FormulaC6 H12 O6
Namebeta-D-fructofuranose;
beta-D-fructose;
D-fructose;
fructose
ChEMBLCHEMBL604608
DrugBank
ZINCZINC000001529270
PDB chain6zaw Chain D Residue 2 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6zaw An unprecedented insight into the catalytic mechanism of copper nitrite reductase from atomic-resolution and damage-free structures.
Resolution1.3 Å
Binding residue
(original residue number in PDB)		P293 G294 W321
Binding residue
(residue number reindexed from 1)		P291 G292 W319
Annotation score1
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).
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:6zaw, PDBe:6zaw, PDBj:6zaw
PDBsum6zaw
PubMed33523860
UniProtH0SLX7

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