Structure of PDB 1fwe Chain C Binding Site BS03

Receptor Information
>1fwe Chain C (length=552) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SNISRQAYADMFGPTVGDKVRLADTELWIEVEDDLTTYGEEVKFGGGKVI
RDGMGQGQMLAADCVDLVLTNALIVDHWGIVKADIGVKDGRIFAIGKAGN
PDIQPNVTIPIGAATEVIAAEGKIVTAGGIDTHIHWICPQQAEEALVSGV
TTMVGGGTGPAAGTHATTCTPGPWYISRMLQAADSLPVNIGLLGKGNVSQ
PDALREQVAAGVIGLKIHEDWGATPAAIDCALTVADEMDIQVALHSDTLN
ESGFVEDTLAAIGGRTIHTFHTEGAGGGHAPDIITACAHPNILPSSTNPT
LPYTLNTIDEHLDMLMFAESRIRRETIAAEDVLHDLGAFSLTSSDSQAMG
RVGEVILRTWQVAHRMKVQRGALAEETGDNDNFRVKRYIAKYTINPALTH
GIAHEVGSIEVGKLADLVVWSPAFFGVKPATVIKGGMIAIAPMGDINASI
PTPQPVHYRPMFGALGSARHHCRLTFLSQAAAANGVAERLNLRSAIAVVK
GCRTVQKADMVHNSLQPNITVDAQTYEVRVDGELITSEPADVLPMAQRYF
LF
Ligand information
Ligand IDHAE
InChIInChI=1S/C2H5NO2/c1-2(4)3-5/h5H,1H3,(H,3,4)
InChIKeyRRUDCFGSUDOHDG-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=C(NO)C
CACTVS 3.341
OpenEye OEToolkits 1.5.0		CC(=O)NO
FormulaC2 H5 N O2
NameACETOHYDROXAMIC ACID
ChEMBLCHEMBL734
DrugBankDB00551
ZINCZINC000004658603
PDB chain1fwe Chain C Residue 989 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1fwe Structures of Cys319 variants and acetohydroxamate-inhibited Klebsiella aerogenes urease.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		H134 K217 H246 G277 D360 A363
Binding residue
(residue number reindexed from 1)		H133 K216 H245 G276 D345 A348
Annotation score1
Binding affinityPDBbind-CN: -logKd/Ki=5.60,Ki=2.5uM
Enzymatic activity
Catalytic site (original residue number in PDB) H134 H136 K217 H219 D221 H246 H272 R336 D360
Catalytic site (residue number reindexed from 1) H133 H135 K216 H218 D220 H245 H271 R321 D345
Enzyme Commision number 3.5.1.5: urease.
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0009039 urease activity
GO:0016151 nickel cation binding
GO:0016787 hydrolase activity
GO:0016810 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
GO:0046872 metal ion binding
Biological Process
GO:0043419 urea catabolic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1fwe, PDBe:1fwe, PDBj:1fwe
PDBsum1fwe
PubMed9201965
UniProtP18314|URE1_KLEAE Urease subunit alpha (Gene Name=ureC)

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