Structure of PDB 1fwx Chain B Binding Site BS01

Receptor Information
>1fwx Chain B (length=589) Species: 266 (Paracoccus denitrificans) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DGSVAPGQLDDYYGFWSSGQSGEMRILGIPSMRELMRVPVFNRCSATGWG
QTNESVRIHERTMSERTKKFLAANGKRIHDNGDLHHVHMSFTEGKYDGRF
LFMNDKANTRVARVRCDVMKCDAILEIPNAKGIHGLRPQKWPRSNYVFCN
GEDETPLVNDGTNMEDVANYVNVFTAVDADKWEVAWQVLVSGNLDNCDAD
YEGKWAFSTSYNSEKGMTLPEMTAAEMDHIVVFNIAEIEKAIAAGDYQEL
NGVKVVDGRKEASSLFTRYIPIANNPHGCNMAPDKKHLCVAGKLSPTVTV
LDVTRFDAVFYENADPRSAVVAEPELGLGPLHTAFDGRGNAYTSLFLDSQ
VVKWNIEDAIRAYAGEKVDPIKDKLDVHYQPGHLKTVMGETLDATNDWLV
CLSKFSKDRFLNVGPLKPENDQLIDISGDKMVLVHDGPTFAEPHDAIAVH
PSILSDIKSVWDRNDPMWAETRAQAEADGVDIDNWTEEVIRDGNKVRVYM
SSVAPSFSIESFTVKEGDEVTVIVTNLDEIDDLTHGFTMGNYGVAMEIGP
QMTSSVTFVAANPGVYWYYCQWFCHALHMEMRGRMLVEP
Ligand information
Ligand IDCA
InChIInChI=1S/Ca/q+2
InChIKeyBHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Ca+2]
FormulaCa
NameCALCIUM ION
ChEMBL
DrugBankDB14577
ZINC
PDB chain1fwx Chain B Residue 4903 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1fwx Revisiting the Catalytic CuZ Cluster of Nitrous Oxide (N2O) Reductase. Evidence of a Bridging Inorganic Sulfur
Resolution1.6 Å
Binding residue
(original residue number in PDB)		Y204 E207 M215 D221 N268
Binding residue
(residue number reindexed from 1)		Y211 E214 M222 D228 N275
Annotation score1
Enzymatic activity
Enzyme Commision number 1.7.2.4: nitrous-oxide reductase.
Gene Ontology
Molecular Function
GO:0004129 cytochrome-c oxidase activity
GO:0005507 copper ion binding
GO:0005509 calcium ion binding
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
GO:0050304 nitrous-oxide reductase activity
Biological Process
GO:0019333 denitrification pathway
GO:1902600 proton transmembrane transport
Cellular Component
GO:0016020 membrane
GO:0042597 periplasmic space

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1fwx, PDBe:1fwx, PDBj:1fwx
PDBsum1fwx
PubMed11024061
UniProtQ51705|NOSZ_PARDE Nitrous-oxide reductase (Gene Name=nosZ)

[Back to BioLiP]