Structure of PDB 1a5o Chain C

Receptor sequence

>1a5oC (length=566)

SNISRQAYADMFGPTVGDKVRLADTELWIEVEDDLTTYGEEVKFGGGKVI
RDGMGQGQMLAADCVDLVLTNALIVDHWGIVKADIGVKDGRIFAIGKAGN
PDIQPNVTIPIGAATEVIAAEGKIVTAGGIDTHIHWICPQQAEEALVSGV
TTMVGGGTGPAAGTHATTCTPGPWYISRMLQAADSLPVNIGLLGKGNVSQ
PDALREQVAAGVIGLCIHEDWGATPAAIDCALTVADEMDIQVALHSDTLN
ESGFVEDTLAAIGGRTIHTFHTEGAGGGHAPDIITACAHPNILPSSTNPT
LPYTLNTIDEHLDMLMVCHHLDPDIAEDVAFAESRIRRETIAAEDVLHDL
GAFSLTSSDSQAMGRVGEVILRTWQVAHRMKVQRGALAEETGDNDNFRVK
RYIAKYTINPALTHGIAHEVGSIEVGKLADLVVWSPAFFGVKPATVIKGG
MIAIAPMGDINASIPTPQPVHYRPMFGALGSARHHCRLTFLSQAAAANGV
AERLNLRSAIAVVKGCRTVQKADMVHNSLQPNITVDAQTYEVRVDGELIT
SEPADVLPMAQRYFLF

3D structure

• PDB: 1a5o Chemical rescue of Klebsiella aerogenes urease variants lacking the carbamylated-lysine nickel ligand.
• Chain: C
• Resolution: 2.5 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H134 H136 C217 H219 D221 H246 H272 H320 R336 D360
• Catalytic site (residue number reindexed from 1): H133 H135 C216 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	H246 H272	H245 H271
BS02	NI	C	H134 H136 D360	H133 H135 D359
BS03	FMT	C	H134 H136 H219 H246 F271	H133 H135 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:1a5o, PDBe:1a5o, PDBj:1a5o
• PDBsum: 1a5o
• PubMed: 9558361
• UniProt: P18314|URE1_KLEAE Urease subunit alpha (Gene Name=ureC)