Structure of PDB 1nq9 Chain I

Receptor sequence
>1nq9I (length=406) Species: 9606 (Homo sapiens) [Search protein sequence]
DICTAKPRDIPMNPMCIYRSPKIPEATNRRVWELSKANSRFATTFYQHLA
DSKNDNDNIFLSPLSISTAFAMTKLGACNDTLQQLMEVFKFDTISEKTSD
QIHFFFAKLNCRLYRKSSKLVSANRLFGDKSLTFNETYQDISELVYGAKL
QPLDFKENAEQSRAAINKWVSNKTEGRITDVIPSEAINELTVLVLVNTIY
FKGLWKSKFSPENTRKELFYKADGESCSASMMYQEGKFRYRRVAEGTQVL
ELPFKGDDITMVLILPKPEKSLAKVEKELTPEVLQEWLDELEEMMLVVHM
PRFRIEDGFSLKEQLQDMGLVDLFSPEKSKLPGIVDLYVSDAFHKAFLEV
NEEGSEAAASTAVVIAGRSLNPNRVTFKANRPFLVFIREVPLNTIIFMGR
VANPCV
3D structure
PDB1nq9 Crystal Structure of Antithrombin in a Heparin-Bound Intermediate State
ChainI
Resolution2.6 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 Z9L I R13 R47 K114 R8 R30 K97
BS02 Z9K I R13 R47 R8 R30
BS03 GU6 I P12 R13 K114 P7 R8 K97
BS04 Z9H I T44 N45 V48 R129 T27 N28 V31 R112
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1nq9, PDBe:1nq9, PDBj:1nq9
PDBsum1nq9
PubMed12873131
UniProtP01008|ANT3_HUMAN Antithrombin-III (Gene Name=SERPINC1)

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