Structure of PDB 1o5c Chain B

Receptor sequence
>1o5cB (length=246) Species: 9606 (Homo sapiens) [Search protein sequence]
IIGGEFTTIENQPWFAAIYRRHRGGSVTYVCGGSLMSPCWVISATHCFID
YPKKEDYIVYLGRSRLNSNTQGEMKFEVENLILHKDYSADTLAHHNDIAL
LKIRSKEGRCAQPSRTIQTICLPSMYNDPQFGTSCEITGFGKEASTDYLY
PEQLKMTVVKLISHRECQQPHYYGSEVTTKMLCAADPQWKTDACQGDSGG
PLVCSLQGRMTLTGIVSWGRGCALKDKPGVYTRVSHFLPWIRSHTK
3D structure
PDB1o5c Dissecting and designing inhibitor selectivity determinants at the S1 site using an artificial Ala190 protease (Ala190 uPA)
ChainB
Resolution1.63 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) H46 D97 Q195 G196 D197 S198 G199
Enzyme Commision number 3.4.21.73: u-plasminogen activator.
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 peptide B N26 W29 P49 P114 R116 Q119 T120 I121 C122 M207 N11 W14 P38 P113 R115 Q118 T119 I120 C121 M210
BS02 CR9 B V41 H57 A190 Q192 S195 V213 G219 V30 H46 A193 Q195 S198 V216 G221 MOAD: Ki=6uM
PDBbind-CN: -logKd/Ki=5.22,Ki=6.0uM
BindingDB: Ki=30nM
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:1o5c, PDBe:1o5c, PDBj:1o5c
PDBsum1o5c
PubMed15522303
UniProtP00749|UROK_HUMAN Urokinase-type plasminogen activator (Gene Name=PLAU)

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