Structure of PDB 6tdt Chain H

Receptor sequence
>6tdtH (length=251) Species: 9606 (Homo sapiens) [Search protein sequence]
IVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPW
DKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDI
ALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKETGQP
SVLQVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSGG
PFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDQF
G
3D structure
PDB6tdt Protein-Induced Change in Ligand Protonation during Trypsin and Thrombin Binding: Hint on Differences in Selectivity Determinants of Both Proteins?
ChainH
Resolution1.53 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 G196
Catalytic site (residue number reindexed from 1) H43 D99 E195 G196 D197 S198 G199
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 H L40 L65 R67 R73 T74 R75 Y76 K81 I82 L26 L60 R62 R68 T69 R70 Y71 K77 I78
BS02 LXW H Y60A W60D N98 L99 I174 A190 E192 S195 S214 W215 G216 G219 Y47 W50 N95 L96 I172 A193 E195 S198 S219 W220 G221 G223 MOAD: Ki=1213nM
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:6tdt, PDBe:6tdt, PDBj:6tdt
PDBsum6tdt
PubMed32011145
UniProtP00734|THRB_HUMAN Prothrombin (Gene Name=F2)

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