Structure of PDB 1eol Chain A

Receptor sequence
>1eolA (length=278) Species: 9606 (Homo sapiens) [Search protein sequence]
GGADCGLRPLFEKKSLEDKTERELLESYIIVEGSDAEIGMSPWQVMLFRK
SPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTENDLLVRIGKHSRTRY
ERNIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHPVCLP
DRETAASLLQAGYKGRVTGWGNLKEGQPSVLQVVNLPIVERPVCKDSTRI
RITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGE
GCDRDGKYGFYTHVFRLKKWIQKVIDQF
3D structure
PDB1eol Design of P1' and P3' residues of trivalent thrombin inhibitors and their crystal structures.
ChainA
Resolution2.1 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) H72 D128 E223 G224 D225 S226 G227
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 A Q38 L40 L41 H57 W60D R73 T74 R75 Y76 I82 L99 D189 A190 C191 E192 W215 G216 G219 Q53 L55 L56 H72 W79 R97 T98 R99 Y100 I107 L125 D220 A221 C222 E223 W248 G249 G251
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
GO:0005509 calcium ion binding
Biological Process
GO:0006508 proteolysis
GO:0007596 blood coagulation
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1eol, PDBe:1eol, PDBj:1eol
PDBsum1eol
PubMed10694407
UniProtP00734|THRB_HUMAN Prothrombin (Gene Name=F2)

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