Structure of PDB 1ycg Chain A Binding Site BS01
Receptor Information
>1ycg Chain A (length=398) Species:
1525
(Moorella thermoacetica) [
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SQPVAITDGIYWVGAVDWNIRYFHGPAFSTHRGTTYNAYLIVDDKTALVD
TVYEPFKEELIAKLKQIKDPVKLDYLVVNHTESDHAGAFPAIMELCPDAH
VLCTQRAFDSLKAHYSHIDFNYTIVKTGTSVSLGKRSLTFIEAPMLHWPD
SMFTYVPEEALLLPNDAFGQHIATSVRFDDQVDAGLIMDEAAKYYANILM
PFSNLITKKLDEIQKINLAIKTIAPSHGIIWRKDPGRIIEAYARWAEGQG
KAKAVIAYDTMWLSTEKMAHALMDGLVAGGCEVKLFKLSVSDRNDVIKEI
LDARAVLVGSPTINNDILPVVSPLLDDLVGLRPKNKVGLAFGAYGWGGGA
QKILEERLKAAKIELIAEPGPTVQWVPRGEDLQRCYELGRKIAARIAD
Ligand information
Ligand ID
ZN
InChI
InChI=1S/Zn/q+2
InChIKey
PTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Zn+2]
Formula
Zn
Name
ZINC ION
ChEMBL
CHEMBL1236970
DrugBank
DB14532
ZINC
PDB chain
1ycg Chain A Residue 402 [
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Receptor-Ligand Complex Structure
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PDB
1ycg
X-ray crystal structures of Moorella thermoacetica FprA. Novel diiron site structure and mechanistic insights into a scavenging nitric oxide reductase.
Resolution
2.8 Å
Binding residue
(original residue number in PDB)
H271 D275
Binding residue
(residue number reindexed from 1)
H270 D274
Annotation score
4
Enzymatic activity
Catalytic site (original residue number in PDB)
H25 H81 E83 D85 H148 D167 Y195 H228
Catalytic site (residue number reindexed from 1)
H24 H80 E82 D84 H147 D166 Y194 H227
Enzyme Commision number
1.-.-.-
Gene Ontology
Molecular Function
GO:0009055
electron transfer activity
GO:0010181
FMN binding
GO:0016491
oxidoreductase activity
GO:0046872
metal ion binding
View graph for
Molecular Function
External links
PDB
RCSB:1ycg
,
PDBe:1ycg
,
PDBj:1ycg
PDBsum
1ycg
PubMed
15850383
UniProt
Q9FDN7
|FPRA_MOOTA Nitric oxide reductase (Gene Name=fprA)
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