Structure of PDB 1ql9 Chain A

Receptor sequence
>1ql9A (length=223) Species: 10116 (Rattus norvegicus) [Search protein sequence]
IVGGYTCQENSVPYQVSLNSGYHFCGGSLINDQWVVSAAHCYKSRIQVRL
GEHNINVLEGNEQFVNAAKIIKHPNFDRETYNNDIMLIKLSSPVKLNARV
ATVALPSSCAPAGTQCLISGWGNTLSSGVNEPDLLQCLDAPLLPQADCEA
SYPGKITDNMVCVGFLEGGKDSCQGDSGGPVVCNGELQGIVSWGYGCALP
DNPGVYTKVCNYVDWIQDTIAAN
3D structure
PDB1ql9 Reconstructing the Binding Site of Factor Xa in Trypsin Reveals Ligand-Induced Structural Plasticity
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H57 D102 Q192 G193 D194 S195 G196
Catalytic site (residue number reindexed from 1) H40 D84 Q174 G175 D176 S177 G178
Enzyme Commision number 3.4.21.4: trypsin.
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 CA A E70 N72 V75 E77 E80 E52 N54 V57 E59 E62
BS02 ZEN A T98 Y99 S190 Q192 V213 W215 G216 Y217 C220 G226 V227 Y228 T80 Y81 S172 Q174 V191 W193 G194 Y195 C197 G204 V205 Y206 MOAD: Ki=4.45uM
PDBbind-CN: -logKd/Ki=5.35,Ki=4.45uM
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
GO:0005509 calcium ion binding
GO:0005515 protein binding
GO:0008236 serine-type peptidase activity
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis
GO:0007584 response to nutrient
GO:0007586 digestion
GO:0030574 collagen catabolic process
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space

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Cellular Component
External links
PDB RCSB:1ql9, PDBe:1ql9, PDBj:1ql9
PDBsum1ql9
PubMed12527302
UniProtP00763|TRY2_RAT Anionic trypsin-2 (Gene Name=Prss2)

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