Structure of PDB 1a5n Chain C

Receptor sequence

>1a5nC (length=551)

SNISRQAYADMFGPTVGDKVRLADTELWIEVEDDLTTYGEEVKFGGGKVI
RDGMGQGQMLAADCVDLVLTNALIVDHWGIVKADIGVKDGRIFAIGKAGN
PDIQPNVTIPIGAATEVIAAEGKIVTAGGIDTHIHWICPQQAEEALVSGV
TTMVGGGTGPAAGTHATTCTPGPWYISRMLQAADSLPVNIGLLGKGNVSQ
PDALREQVAAGVIGLAIHEDWGATPAAIDCALTVADEMDIQVALHSDTLN
ESGFVEDTLAAIGGRTIHTFHTEGAGGGHAPDIITACAHPNILPSSTNPT
LPYTLNTIDEHLDMAFAESRIRRETIAAEDVLHDLGAFSLTSSDSQAMGR
VGEVILRTWQVAHRMKVQRGALAEETGDNDNFRVKRYIAKYTINPALTHG
IAHEVGSIEVGKLADLVVWSPAFFGVKPATVIKGGMIAIAPMGDINASIP
TPQPVHYRPMFGALGSARHHCRLTFLSQAAAANGVAERLNLRSAIAVVKG
CRTVQKADMVHNSLQPNITVDAQTYEVRVDGELITSEPADVLPMAQRYFL
F

3D structure

• PDB: 1a5n Chemical rescue of Klebsiella aerogenes urease variants lacking the carbamylated-lysine nickel ligand.
• Chain: C
• Resolution: 2.4 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H134 H136 A217 H219 D221 H246 H272 R336 D360
• Catalytic site (residue number reindexed from 1): H133 H135 A216 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	H219 H246 H272	H218 H245 H271
BS02	NI	C	H134 H136 D360	H133 H135 D344
BS03	FMT	C	H134 H136 T169 H219 H246 F271	H133 H135 T168 H218 H245 F270

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:1a5n, PDBe:1a5n, PDBj:1a5n
• PDBsum: 1a5n
• PubMed: 9558361
• UniProt: P18314|URE1_KLEAE Urease subunit alpha (Gene Name=ureC)