Structure of PDB 1jvq Chain I Binding Site BS01

Receptor Information

>1jvq Chain I (length=410) Species: 9606 (Homo sapiens)

VDICTAKPRDIPMNPMCIYRSPEEATNRRVWELSKANSRFATTFYQHLAD
SKNDNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTISEKTSDQ
IHFFFAKLNCRLYRKANKSSKLVSANRLFGDKSLTFNETYQDISELVYGA
KLQPLDFKENAEQSRAAINKWVSNKTEGRITDVIPSEAINELTVLVLVNT
IYFKGLWKSKFSPENTRKELFYKADGESCSASMMYQEGKFRYRRVAEGTQ
VLELPFKGDDITMVLILPKPEKSLAKVEKELTPEVLQEWLDELEEMMLVV
HMPRFRIEDGFSLKEQLQDMGLVDLFSPEKSKLPGIVAEGRDDLYVSDAF
HKAFLEVNEEGSASTAVVIAGRSLNPNRVTFKANRPFLVFIREVPLNTII
FMGRVANPCV

Ligand information

>1jvq Chain C (length=7)

SEAAAST

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1jvq How small peptides block and reverse serpin polymerisation
• Resolution: 2.6 Å
• Binding residue (original residue number in PDB): S82 I83 V190 R197 I198 V216 N217 T218 I219 Y220 F221 K222 G223 W225 F274 F368 H369 K370 A371 F372 L373 E374 V375 N376 F422
• Binding residue (residue number reindexed from 1): S64 I65 V172 R179 I180 V198 N199 T200 I201 Y202 F203 K204 G205 W207 F256 F350 H351 K352 A353 F354 L355 E356 V357 N358 F401

Gene Ontology

Molecular Function

• GO:0002020 protease binding
• GO:0004867 serine-type endopeptidase inhibitor activity
• GO:0005515 protein binding
• GO:0008201 heparin binding
• GO:0042802 identical protein binding

Biological Process

• GO:0007596 blood coagulation
• GO:0010466 negative regulation of peptidase activity
• GO:0030193 regulation of blood coagulation

Cellular Component

• GO:0005576 extracellular region
• GO:0005615 extracellular space
• GO:0005788 endoplasmic reticulum lumen
• GO:0005886 plasma membrane
• GO:0062023 collagen-containing extracellular matrix
• GO:0070062 extracellular exosome
• GO:0072562 blood microparticle

External links

• PDB: RCSB:1jvq, PDBe:1jvq, PDBj:1jvq
• PDBsum: 1jvq
• PubMed: 15342247
• UniProt: P01008|ANT3_HUMAN Antithrombin-III (Gene Name=SERPINC1)