Structure of PDB 3qgk Chain F

Receptor sequence
>3qgkF (length=564) Species: 679897 (Helicobacter mustelae 12198) [Search protein sequence]
MKMKRQEYVNTYGPTTGDKVRLGDTDLWAEVEHDYTVYGEELKFGAGKTI
REGMGQSNSPDENTLDLVITNALIIDYTGIYKADIGIKNGKIHGIGKAGN
KDMQDGVTPHMVVGVGTEALAGEGMIITAGGIDSHTHFLSPQQFPTALAN
GVTTMFGGGTGPVDGTNATTITPGVWNLHRMLRAAEEYGMNVGLLGKGNS
SSRAQLVEQVKAGAIGFKLHEDWGTTPSAIDHCLSVADEYDVQVCIHTDT
VNEAGYVDDTLRAMNGRAIHAYHIEGAGGGHSPDVITMAGEVNILPSSTT
PTIPYTINTVAEHLDMLMTCHHLDKRIRFSQSRIRPGSIAAEDTLHDMGV
IAMTSSDSQAMGRAGEVIPRTWQTADKNKKEFGRLTEEKGDNDNFRIKRY
ISKYTINPAITHGVSEYIGSVEEGKIADLVVWNPAFFGVKPKIIIKGGMV
VFSEMGDSNASVPTPQPVYYREMFGHHGKAKFDTSITFVSKVAYENGIKE
KLGLERKVLPVKNCRNVTKKDFKFNNTTAKITVNPETFEVFVNGKLCTSK
PATEVALASRYTFF
3D structure
PDB3qgk Iron-containing urease in a pathogenic bacterium.
ChainF
Resolution3.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H135 H137 K218 H220 D222 H247 H273 H321 R337 D361
Catalytic site (residue number reindexed from 1) H135 H137 K218 H220 D222 H247 H273 H321 R333 D357
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 FE F K218 H220 H247 H273 K218 H220 H247 H273
BS02 FE F H135 H137 K218 D361 H135 H137 K218 D357
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
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Cellular Component
External links
PDB RCSB:3qgk, PDBe:3qgk, PDBj:3qgk
PDBsum3qgk
PubMed21788478
UniProtD3UJ80

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