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1P0S

Crystal Structure of Blood Coagulation Factor Xa in Complex with Ecotin M84R

Functional Information from GO Data
ChainGOidnamespacecontents
E0004867molecular_functionserine-type endopeptidase inhibitor activity
E0005515molecular_functionprotein binding
E0006952biological_processdefense response
E0030288cellular_componentouter membrane-bounded periplasmic space
E0030414molecular_functionpeptidase inhibitor activity
E0042597cellular_componentperiplasmic space
E0042803molecular_functionprotein homodimerization activity
H0004252molecular_functionserine-type endopeptidase activity
H0006508biological_processproteolysis
L0005509molecular_functioncalcium ion binding
L0005576cellular_componentextracellular region
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG L 139
ChainResidue
EGLN5
LCGU16
LCGU26

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG L 140
ChainResidue
LCGU14
LCGU19
LHOH148

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG L 141
ChainResidue
LCGU25
LCGU29
LHOH144

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG H 265
ChainResidue
HASP70
HASN72
HGLN75
HGLU76
HGLU80
HHOH273

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA H 266
ChainResidue
HTYR185
HASP185
HARG222
HLYS224

Functional Information from PROSITE/UniProt
site_idPS00010
Number of Residues12
DetailsASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CkDglgeYtCtC
ChainResidueDetails
LCYS61-CYS72

site_idPS00011
Number of Residues26
DetailsGLA_1 Vitamin K-dependent carboxylation domain. EcmEEtCsyeearEvfedsdktne.FW
ChainResidueDetails
LCGU16-TRP41

site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CtCleGfeGKnC
ChainResidueDetails
LCYS70-CYS81

site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
HLEU53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DAcqGDSGGPHV
ChainResidueDetails
HASP189-VAL200

site_idPS01186
Number of Residues12
DetailsEGF_2 EGF-like domain signature 2. CtCleGFegkn....C
ChainResidueDetails
LCYS70-CYS81
LCYS109-CYS124

site_idPS01187
Number of Residues25
DetailsEGF_CA Calcium-binding EGF-like domain signature. DgDQCetsp..........Cqnqgk..CkDglgeYtC
ChainResidueDetails
LASP46-CYS70

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsSITE: Reactive bond
ChainResidueDetails
EARG84
LCGU32
LCGU39
HASP102
HSER195
LCGU16
LCGU19
LCGU20
LCGU25
LCGU26
LCGU29

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: (3R)-3-hydroxyaspartate => ECO:0000269|PubMed:6871167
ChainResidueDetails
LASP63

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
HASP102
HHIS57

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
HSER195
HGLY196

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
HSER195
HGLY193

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
HASP102
HSER195
HHIS57

site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
HASP102
HSER195
HGLY193
HHIS57

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
HSER195
HASP100
HGLY193
HHIS57

site_idCSA7
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
HASP102
HSER195
HHIS57
HGLY196

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PDB entries from 2025-06-11

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