Structure of PDB 1g37 Chain A

Receptor sequence
>1g37A (length=277) Species: 9606 (Homo sapiens) [Search protein sequence]
ADCGLRPLFEKKSLEDKTERELLESYIIVEGSDAEIGMSPWQVMLFRKSP
QELLCGASLISDRWVLTAAHCLLYPPWDKNFTENDLLVRIGKHSRTRYER
NIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHPVCLPDR
ETAASLLQAGYKGRVTGWGNLKETGQPSVLQVVNLPIVERPVCKDSTRIR
ITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEG
CDRDGKYGFYTHVFRLKKWIQKVIDQF
3D structure
PDB1g37 Potent and selective bicyclic lactam inhibitors of thrombin. Part 4: transition state inhibitors.
ChainA
Resolution2.0 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) H70 D126 E222 G223 D224 S225 G226
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 F34 K36 R67 T74 R75 Y76 F46 K48 R89 T96 R97 Y98
BS02 110 A L40 L41 H57 W60D E97A N98 L99 I174 A190 E192 G193 S195 W215 G216 G219 L53 L54 H70 W77 E121 N122 L123 I199 A220 E222 G223 S225 W247 G248 G250 PDBbind-CN: -logKd/Ki=10.00,IC50=0.1nM
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:1g37, PDBe:1g37, PDBj:1g37
PDBsum1g37
PubMed11212093
UniProtP00734|THRB_HUMAN Prothrombin (Gene Name=F2)

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