Structure of PDB 6pxj Chain B

Receptor sequence
>6pxjB (length=245) Species: 9606 (Homo sapiens) [Search protein sequence]
TVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPW
DKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDI
ALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNSVLQVVN
LPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSP
FNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDQFGE
3D structure
PDB6pxj Role of the I16-D194 ionic interaction in the trypsin fold.
ChainB
Resolution1.7 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 E192 G193 D194 S195
Catalytic site (residue number reindexed from 1) H43 D99 E188 G189 D190 S191
Enzyme Commision number 3.4.21.5: thrombin.
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 E23 G25 M26 P28 W29 D116 H119 P120 C122 Y134 K135 R137 N159 M201 K202 N205 R206 W207 E8 G10 M11 P13 W14 D113 H116 P117 C119 Y134 K135 R137 N150 M197 K198 N203 R204 W205
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
GO:0005509 calcium ion binding
Biological Process
GO:0006508 proteolysis
GO:0007596 blood coagulation

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6pxj, PDBe:6pxj, PDBj:6pxj
PDBsum6pxj
PubMed31792294
UniProtP00734|THRB_HUMAN Prothrombin (Gene Name=F2)

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