Structure of PDB 1fwb Chain C

Receptor sequence

>1fwbC (length=566)

SNISRQAYADMFGPTVGDKVRLADTELWIEVEDDLTTYGEEVKFGGGKVI
RDGMGQGQMLAADCVDLVLTNALIVDHWGIVKADIGVKDGRIFAIGKAGN
PDIQPNVTIPIGAATEVIAAEGKIVTAGGIDTHIHWICPQQAEEALVSGV
TTMVGGGTGPAAGTHATTCTPGPWYISRMLQAADSLPVNIGLLGKGNVSQ
PDALREQVAAGVIGLKIHEDWGATPAAIDCALTVADEMDIQVALHSDTLN
ESGFVEDTLAAIGGRTIHTFHTEGAGGGHAPDIITACAHPNILPSSTNPT
LPYTLNTIDEHLDMLMVAHHLDPDIAEDVAFAESRIRRETIAAEDVLHDL
GAFSLTSSDSQAMGRVGEVILRTWQVAHRMKVQRGALAEETGDNDNFRVK
RYIAKYTINPALTHGIAHEVGSIEVGKLADLVVWSPAFFGVKPATVIKGG
MIAIAPMGDINASIPTPQPVHYRPMFGALGSARHHCRLTFLSQAAAANGV
AERLNLRSAIAVVKGCRTVQKADMVHNSLQPNITVDAQTYEVRVDGELIT
SEPADVLPMAQRYFLF

3D structure

• PDB: 1fwb 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 H320 R336 D360
• Catalytic site (residue number reindexed from 1): H133 H135 K216 H218 D220 H245 H271 H319 R335 D359
• 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 D359

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