Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2AFQ

1.9 angstrom crystal structure of wild-type human thrombin in the sodium free state

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 PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL D 1001
ChainResidue
DHIS57
DTYR60
DLEU99
DHOH302
DHOH413
DHOH602
DHOH634
DHOH637
DHOH761

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 1002
ChainResidue
BHIS57
BTYR60
BGLU192
BTRP215
BHOH336
BHOH552
BHOH612
BHOH640

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL D 1003
ChainResidue
DPRO111
DPRO166
DASP170

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 1004
ChainResidue
BALA129
BHIS230
BPHE232
BARG233
BHOH648

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 1005
ChainResidue
BPHE34
BGLN38
BARG67
BARG73
BHOH464
BHOH642

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GOL D 1006
ChainResidue
DASP116

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL D 1007
ChainResidue
BASP222
BHOH369
DLEU41
DCYS42
DHIS57
DLYS60
DGLU192
DGLY193
DSER195
DHOH522

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 Residues6
DetailsACT_SITE: Charge relay system
ChainResidueDetails
BHIS57
BASP102
BSER195
DHIS57
DASP102
DSER195

site_idSWS_FT_FI2
Number of Residues2
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
DASN60

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

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
BSER195
BGLY193

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
DSER195
DGLY193

site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BASP102
BSER195
BHIS57
BGLY196

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
DASP102
DSER195
DHIS57
DGLY196

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BASP102
BSER195
BHIS57

site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
DASP102
DSER195
DHIS57

226262

PDB entries from 2024-10-16

PDB statisticsPDBj update infoContact PDBjnumon