Structure of PDB 1jvq Chain I Binding Site BS02

Receptor Information

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

VDICTAKPRDIPMNPMCIYRSPEEATNRRVWELSKANSRFATTFYQHLAD
SKNDNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTISEKTSDQ
IHFFFAKLNCRLYRKANKSSKLVSANRLFGDKSLTFNETYQDISELVYGA
KLQPLDFKENAEQSRAAINKWVSNKTEGRITDVIPSEAINELTVLVLVNT
IYFKGLWKSKFSPENTRKELFYKADGESCSASMMYQEGKFRYRRVAEGTQ
VLELPFKGDDITMVLILPKPEKSLAKVEKELTPEVLQEWLDELEEMMLVV
HMPRFRIEDGFSLKEQLQDMGLVDLFSPEKSKLPGIVAEGRDDLYVSDAF
HKAFLEVNEEGSASTAVVIAGRSLNPNRVTFKANRPFLVFIREVPLNTII
FMGRVANPCV

Ligand information

>1jvq Chain D (length=4)

WMDF

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): F87 T90 V201 I202 A206 V212 L213 V214 L215 L351 V364 S365 D366 A367 F368
• Binding residue (residue number reindexed from 1): F69 T72 V183 I184 A188 V194 L195 V196 L197 L333 V346 S347 D348 A349 F350

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)