Structure of PDB 1gja Chain B

Receptor sequence
>1gjaB (length=245) Species: 9606 (Homo sapiens) [Search protein sequence]
IIGGEFTTIENQPWFAAIYRRHRGGSVTYVCGGSLMSPCWVISATHCFID
YPKKEDYIVYLGRSRLNSNTQGEMKFEVENLILHKDYSADTLAHHNDIAL
LKIRSKEGRCAQPSRTIQTICLPSMYNDPQFGTSCEITGFGKEASTDYLY
PEQLKMTVVKLISHRECQQPHYYGSEVTTKMLCAADPQWKTDSCQGDSGG
PLVCSLQGRMTLTGIVSWGRGCALKDKPGVYTRVSHFLPWIRSHT
3D structure
PDB1gja Engineering inhibitors highly selective for the S1 sites of Ser190 trypsin-like serine protease drug targets.
ChainB
Resolution1.56 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 A112 Q113 P114 Q119 T120 I121 C122 N11 W14 A111 Q112 P113 Q118 T119 I120 C121
BS02 135 B H57 D189 S190 C191 Q192 G193 S195 G219 C220 H46 D192 S193 C194 Q195 G196 S198 G221 C222 MOAD: Ki=3.8uM
PDBbind-CN: -logKd/Ki=5.42,Ki=3.8uM
BindingDB: Ki=2700nM
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:1gja, PDBe:1gja, PDBj:1gja
PDBsum1gja
PubMed11731301
UniProtP00749|UROK_HUMAN Urokinase-type plasminogen activator (Gene Name=PLAU)

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