Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3HK6

Crystal structure of murine thrombin mutant W215A/E217A (two molecules in the asymmetric unit)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0005576cellular_componentextracellular region
A0006508biological_processproteolysis
A0007596biological_processblood coagulation
B0004252molecular_functionserine-type endopeptidase activity
B0005509molecular_functioncalcium ion binding
B0006508biological_processproteolysis
B0007596biological_processblood coagulation
C0004252molecular_functionserine-type endopeptidase activity
C0005576cellular_componentextracellular region
C0006508biological_processproteolysis
C0007596biological_processblood coagulation
D0004252molecular_functionserine-type endopeptidase activity
D0005509molecular_functioncalcium ion binding
D0006508biological_processproteolysis
D0007596biological_processblood coagulation
Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
BLEU53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DAceGDSGGPFV
ChainResidueDetails
BASP189-VAL200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues508
DetailsDomain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues44
DetailsRegion: {"description":"High affinity receptor-binding region which is also known as the TP508 peptide","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsActive site: {"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"17330941","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BASP102
BSER195
BGLY193
BHIS57

site_idCSA10
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
DASP102
DSER195
DHIS57

site_idCSA11
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BASP102
BSER195
BHIS57
BGLY196

site_idCSA12
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
DASP102
DSER195
DHIS57
DGLY196

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
DASP102
DSER195
DGLY193
DHIS57

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BASP102
BHIS57

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
DASP102
DHIS57

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BSER195
BGLY193

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
DSER195
DGLY193

site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BSER195
BGLY196

site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
DSER195
DGLY196

site_idCSA9
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BASP102
BSER195
BHIS57

247035

PDB entries from 2026-01-07

PDB statisticsPDBj update infoContact PDBjnumon