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1BHX

X-RAY STRUCTURE OF THE COMPLEX OF HUMAN ALPHA THROMBIN WITH THE INHIBITOR SDZ 229-357

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
F0004252molecular_functionserine-type endopeptidase activity
F0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE R56 F 1
ChainResidue
BHIS57
FGLY216
FGLU217
FGLY219
FGLY226
FHOH248
BTYR60
BGLU97
FASP189
FALA190
FCYS191
FSER195
FSER214
FTRP215

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
FASP189-VAL200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Charge relay system
ChainResidueDetails
FSER195
BASP102

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
BASN60

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hja
ChainResidueDetails
FSER195
FGLY193

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1hja
ChainResidueDetails
FSER195
FGLY196
BASP102
BHIS57

221716

PDB entries from 2024-06-26

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