Structure of PDB 1sfq Chain B

Receptor sequence
>1sfqB (length=251) Species: 9606 (Homo sapiens) [Search protein sequence]
IVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPW
DKNFTENDLLVRIGKHSRTRYEANIEKISMLEKIYIHPRYNWRENLDRDI
ALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKETWGQ
PSVLQVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSG
GPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDQ
F
3D structure
PDB1sfq Molecular dissection of na+ binding to thrombin.
ChainB
Resolution1.91 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 E196 G197 D198 S199 G200
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 G25 M26 P28 W29 D116 H119 C122 Y134 K135 R137 N159 K202 N205 R206 W207 Y208 E8 G10 M11 P13 W14 D113 H116 C119 Y134 K135 R137 N158 K206 N211 R212 W213 Y214
BS02 0G6 B H57 Y60A L99 D189 A190 G193 S195 W215 G216 H43 Y47 L96 D193 A194 G197 S199 W221 G222
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:1sfq, PDBe:1sfq, PDBj:1sfq
PDBsum1sfq
PubMed15152000
UniProtP00734|THRB_HUMAN Prothrombin (Gene Name=F2)

[Back to BioLiP]