Structure of PDB 2afq Chain D

Receptor sequence
>2afqD (length=238) Species: 9606 (Homo sapiens) [Search protein sequence]
IVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPW
DKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDI
ALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGPSVLQVVN
LPIVERPVCKDSTRIRITDNMFCAGYKPRGDACEGDSGGPFVMKSPFNNR
WYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDQ
3D structure
PDB2afq Crystal structure of wild-type human thrombin in the Na+-free state
ChainD
Resolution1.93 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 E184 G185 D186 S187 G188
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 D E23 G25 M26 W29 F114 H119 P120 C122 L129C Y134 K135 R137 N159 M201 K202 P204 R206 W207 E8 G10 M11 W14 F111 H116 P117 C119 L129 Y134 K135 R137 N150 M193 K194 P196 R200 W201
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
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Biological Process
External links
PDB RCSB:2afq, PDBe:2afq, PDBj:2afq
PDBsum2afq
PubMed16201969
UniProtP00734|THRB_HUMAN Prothrombin (Gene Name=F2)

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