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5TO3

Crystal structure of thrombin mutant W215A/E217A fused to EGF456 of thrombomodulin via a 31-residue linker and bound to PPACK

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0005576cellular_componentextracellular region
A0006508biological_processproteolysis
A0007596biological_processblood coagulation
B0004252molecular_functionserine-type endopeptidase activity
B0004888molecular_functiontransmembrane signaling receptor activity
B0005509molecular_functioncalcium ion binding
B0006508biological_processproteolysis
B0016020cellular_componentmembrane
Functional Information from PROSITE/UniProt
site_idPS00010
Number of Residues12
DetailsASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. ChNlpgtFeCiC
ChainResidueDetails
BCYS437-CYS448

site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
BLEU54-CYS59

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DAceGDSGGPFV
ChainResidueDetails
BASP214-VAL225

site_idPS01186
Number of Residues15
DetailsEGF_2 EGF-like domain signature 2. CeCpeGYilddgfi.C
ChainResidueDetails
BCYS407-CYS421

site_idPS01187
Number of Residues24
DetailsEGF_CA Calcium-binding EGF-like domain signature. DiDECenggf.........Csgv....ChNlpgtFeC
ChainResidueDetails
BASP423-CYS446

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Charge relay system
ChainResidueDetails
BHIS58
BASP114
BSER220

site_idSWS_FT_FI2
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:873923
ChainResidueDetails
BASN68

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
BASN364
BASN391

224201

PDB entries from 2024-08-28

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