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1ANT

BIOLOGICAL IMPLICATIONS OF A 3 ANGSTROMS STRUCTURE OF DIMERIC ANTITHROMBIN

Functional Information from GO Data
ChainGOidnamespacecontents
I0002020molecular_functionprotease binding
I0004867molecular_functionserine-type endopeptidase inhibitor activity
I0005515molecular_functionprotein binding
I0005576cellular_componentextracellular region
I0005615cellular_componentextracellular space
I0005788cellular_componentendoplasmic reticulum lumen
I0005886cellular_componentplasma membrane
I0007596biological_processblood coagulation
I0007599biological_processhemostasis
I0008201molecular_functionheparin binding
I0030193biological_processregulation of blood coagulation
I0030414molecular_functionpeptidase inhibitor activity
I0042802molecular_functionidentical protein binding
I0062023cellular_componentcollagen-containing extracellular matrix
I0070062cellular_componentextracellular exosome
I0072562cellular_componentblood microparticle
L0002020molecular_functionprotease binding
L0004867molecular_functionserine-type endopeptidase inhibitor activity
L0005515molecular_functionprotein binding
L0005576cellular_componentextracellular region
L0005615cellular_componentextracellular space
L0005788cellular_componentendoplasmic reticulum lumen
L0005886cellular_componentplasma membrane
L0007596biological_processblood coagulation
L0007599biological_processhemostasis
L0008201molecular_functionheparin binding
L0030193biological_processregulation of blood coagulation
L0030414molecular_functionpeptidase inhibitor activity
L0042802molecular_functionidentical protein binding
L0062023cellular_componentcollagen-containing extracellular matrix
L0070062cellular_componentextracellular exosome
L0072562cellular_componentblood microparticle
Functional Information from PROSITE/UniProt
site_idPS00284
Number of Residues11
DetailsSERPIN Serpins signature. FKANRPFLVfI
ChainResidueDetails
LPHE402-ILE412

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING:
ChainResidueDetails
LTRP49
LARG129
LARG145
ITRP49
IARG129
IARG145

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Reactive bond => ECO:0000269|PubMed:7238875
ChainResidueDetails
LARG393
IARG393

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by FAM20C => ECO:0000269|PubMed:26091039
ChainResidueDetails
LTHR31
ITHR31

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039, ECO:0007744|PubMed:24275569
ChainResidueDetails
LSER36
ISER36

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|Ref.10
ChainResidueDetails
IASN96
LASN96

site_idSWS_FT_FI6
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|Ref.10
ChainResidueDetails
LASN135
IASN135

site_idSWS_FT_FI7
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|Ref.10
ChainResidueDetails
LASN155
IASN155

site_idSWS_FT_FI8
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|Ref.10
ChainResidueDetails
LASN192
IASN192

218500

PDB entries from 2024-04-17

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