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5PAT

Crystal Structure of Factor VIIa in complex with N-(2-amino-1H-benzimidazol-5-yl)-2-(3-chlorophenyl)acetamide

Functional Information from GO Data
ChainGOidnamespacecontents
B0004252molecular_functionserine-type endopeptidase activity
B0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue 7ZG B 501
ChainResidue
BHIS253
BTRP424
BGLY425
BGLY427
BCYS428
BSO4502
BHOH608
BHOH744
BGLY297
BTHR298
BASP302
BASP398
BSER399
BCYS400
BSER404
BSER423

site_idAC2
Number of Residues8
Detailsbinding site for residue SO4 B 502
ChainResidue
BHIS253
BLYS401
BGLY402
BSER404
B7ZG501
BHOH673
BHOH691
BHOH726

site_idAC3
Number of Residues7
Detailsbinding site for residue SO4 B 503
ChainResidue
BMET366
BTHR367
BARG439
BHOH627
BHOH635
BHOH679
BHOH700

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VSAAHC
ChainResidueDetails
BVAL249-CYS254

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DSckGDSGGPHA
ChainResidueDetails
BASP398-ALA409

site_idPS01186
Number of Residues16
DetailsEGF_2 EGF-like domain signature 2. CrCheGYslladgvsC
ChainResidueDetails
ACYS172-CYS187

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Charge relay system => ECO:0000250
ChainResidueDetails
BHIS253
BASP302
BSER404

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
BASP398

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19167329, ECO:0000269|PubMed:3264725
ChainResidueDetails
BASN382

224572

PDB entries from 2024-09-04

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