1TB6

2.5A Crystal Structure of the Antithrombin-Thrombin-Heparin Ternary Complex

Functional Information from GO Data

Chain	GOid	namespace	contents
H	0004252	molecular_function	serine-type endopeptidase activity
H	0005509	molecular_function	calcium ion binding
H	0006508	biological_process	proteolysis
H	0007596	biological_process	blood coagulation
I	0002020	molecular_function	protease binding
I	0004867	molecular_function	serine-type endopeptidase inhibitor activity
I	0005515	molecular_function	protein binding
I	0005576	cellular_component	extracellular region
I	0005615	cellular_component	extracellular space
I	0005788	cellular_component	endoplasmic reticulum lumen
I	0005886	cellular_component	plasma membrane
I	0007596	biological_process	blood coagulation
I	0008201	molecular_function	heparin binding
I	0010466	biological_process	negative regulation of peptidase activity
I	0030193	biological_process	regulation of blood coagulation
I	0042802	molecular_function	identical protein binding
I	0062023	cellular_component	collagen-containing extracellular matrix
I	0070062	cellular_component	extracellular exosome
I	0072562	cellular_component	blood microparticle
L	0004252	molecular_function	serine-type endopeptidase activity
L	0005576	cellular_component	extracellular region
L	0006508	biological_process	proteolysis
L	0007596	biological_process	blood coagulation

Functional Information from PROSITE/UniProt

site_id	PS00134
Number of Residues	6
Details	TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC

Chain	Residue	Details
H	LEU53-CYS58

site_id	PS00284
Number of Residues	11
Details	SERPIN Serpins signature. FKANRPFLVfI

Chain	Residue	Details
I	PHE402-ILE412

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI2
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269\|PubMed:16335952, ECO:0000269\|PubMed:19139490, ECO:0000269\|PubMed:19159218, ECO:0000269\|PubMed:19838169, ECO:0000269\|PubMed:873923

Chain	Residue	Details
H	ASN60

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by FAM20C => ECO:0000269\|PubMed:26091039

Chain	Residue	Details
I	THR31

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine; by FAM20C => ECO:0000269\|PubMed:26091039, ECO:0007744\|PubMed:24275569

Chain	Residue	Details
I	SER36

site_id	SWS_FT_FI5
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:14760718, ECO:0000269\|PubMed:16335952, ECO:0000269\|PubMed:19159218, ECO:0000269\|Ref.10

Chain	Residue	Details
I	ASN96

site_id	SWS_FT_FI6
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|Ref.10

Chain	Residue	Details
I	ASN135

site_id	SWS_FT_FI7
Number of Residues	1
Details	CARBOHYD: 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

Chain	Residue	Details
I	ASN155

site_id	SWS_FT_FI8
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:16263699, ECO:0000269\|PubMed:16335952, ECO:0000269\|Ref.10

Chain	Residue	Details
I	ASN192

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1a0j

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1a0j

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1a0j

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

site_id	CSA5
Number of Residues	3
Details	Annotated By Reference To The Literature 1a0j