Structure of PDB 1fwf Chain C

Receptor sequence

>1fwfC (length=551)

SNISRQAYADMFGPTVGDKVRLADTELWIEVEDDLTTYGEEVKFGGGKVI
RDGMGQGQMLAADCVDLVLTNALIVDHWGIVKADIGVKDGRIFAIGKAGN
PDIQPNVTIPIGAATEVIAAEGKIVTAGGIDTHIHWICPQQAEEALVSGV
TTMVGGGTGPAAGTHATTCTPGPWYISRMLQAADSLPVNIGLLGKGNVSQ
PDALREQVAAGVIGLKIHEDWGATPAAIDCALTVADEMDIQVALHSDTLN
ESGFVEDTLAAIGGRTIHTFHTEGAGGGHAPDIITACAHPNILPSSTNPT
LPYTLNTIDEHLDMLFAESRIRRETIAAEDVLHDLGAFSLTSSDSQAMGR
VGEVILRTWQVAHRMKVQRGALAEETGDNDNFRVKRYIAKYTINPALTHG
IAHEVGSIEVGKLADLVVWSPAFFGVKPATVIKGGMIAIAPMGDINASIP
TPQPVHYRPMFGALGSARHHCRLTFLSQAAAANGVAERLNLRSAIAVVKG
CRTVQKADMVHNSLQPNITVDAQTYEVRVDGELITSEPADVLPMAQRYFL
F

3D structure

• PDB: 1fwf Structures of Cys319 variants and acetohydroxamate-inhibited Klebsiella aerogenes urease.
• Chain: C
• Resolution: 2.0 Å

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 R320 D344
• Enzyme Commision number: 3.5.1.5: urease.

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	NI	C	K217 H246 H272	K216 H245 H271
BS02	NI	C	H134 H136 K217 D360	H133 H135 K216 D344

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

External links

• PDB: RCSB:1fwf, PDBe:1fwf, PDBj:1fwf
• PDBsum: 1fwf
• PubMed: 9201965
• UniProt: P18314|URE1_KLEAE Urease subunit alpha (Gene Name=ureC)