Structure of PDB 6hsx Chain H

Receptor sequence

>6hsxH (length=250) Species: 9606 (Homo sapiens) [Search protein sequence]

IVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPW
DKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDI
ALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKETGQP
SVLQVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSGG
PFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDQF

3D structure

PDB

6hsx Protein-Induced Change in Ligand Protonation during Trypsin and Thrombin Binding: Hint on Differences in Selectivity Determinants of Both Proteins?

Chain

Resolution

1.56 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 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)
BS01	peptide	H	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 N157 M204 K205 N210 R211 W212
BS02	peptide	H	L40 R67 R73 T74 R75 Y76 I82	L26 R62 R68 T69 R70 Y71 I78
BS03	GOZ	H	Y60A W60D E192 S195 S214 W215 G216 G219	Y47 W50 E195 S198 S219 W220 G221 G223

Gene Ontology

	Molecular Function
GO:0004252	serine-type endopeptidase activity
GO:0005509	calcium ion binding

	Biological Process
GO:0006508	proteolysis
GO:0007596	blood coagulation

View graph for
Molecular Function

View graph for
Biological Process

External links

PDB	RCSB:6hsx, PDBe:6hsx, PDBj:6hsx
PDBsum	6hsx
PubMed	32011145
UniProt	P00734\|THRB_HUMAN Prothrombin (Gene Name=F2)

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