Structure of PDB 1twx Chain B

Receptor sequence
>1twxB (length=252) Species: 9606 (Homo sapiens) [Search protein sequence]
IVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPW
DKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDI
ALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKETGQP
SVLQVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSGG
PFVMKSPFNNRWYQMGIVSWGEGCARKGKYGFYTHVFRLKKWIQKVIDQF
GE
3D structure
PDB1twx Crystal structure of the thrombin mutant D221A/D222K: the Asp222:Arg187 ion-pair stabilizes the fast form
ChainB
Resolution2.4 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 B E23 I24 M26 P28 W29 D116 H119 P120 C122 L129C Y134 K135 R137 N159 K202 R206 W207 E8 I9 M11 P13 W14 D113 H116 P117 C119 L129 Y134 K135 R137 N157 K205 R211 W212
BS02 peptide B Q38 R67 R73 T74 R75 Y76 K81 I82 Q24 R62 R68 T69 R70 Y71 K77 I78
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:1twx, PDBe:1twx, PDBj:1twx
PDBsum1twx
PubMed15572256
UniProtP00734|THRB_HUMAN Prothrombin (Gene Name=F2)

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