1SR5

ANTITHROMBIN-ANHYDROTHROMBIN-HEPARIN TERNARY COMPLEX STRUCTURE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0002020	molecular_function	protease binding
A	0004867	molecular_function	serine-type endopeptidase inhibitor activity
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0005788	cellular_component	endoplasmic reticulum lumen
A	0005886	cellular_component	plasma membrane
A	0007596	biological_process	blood coagulation
A	0008201	molecular_function	heparin binding
A	0030193	biological_process	regulation of blood coagulation
A	0042802	molecular_function	identical protein binding
A	0062023	cellular_component	collagen-containing extracellular matrix
A	0070062	cellular_component	extracellular exosome
A	0072562	cellular_component	blood microparticle
B	0004252	molecular_function	serine-type endopeptidase activity
B	0005576	cellular_component	extracellular region
B	0006508	biological_process	proteolysis
B	0007596	biological_process	blood coagulation
C	0004252	molecular_function	serine-type endopeptidase activity
C	0005509	molecular_function	calcium ion binding
C	0006508	biological_process	proteolysis
C	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
C	LEU53-CYS58

site_id	PS00135
Number of Residues	12
Details	TRYPSIN_SER Serine proteases, trypsin family, serine active site. DAceGDSGGPFV

Chain	Residue	Details
C	ASP189-VAL200

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

Chain	Residue	Details
A	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
C	ASN60

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

Chain	Residue	Details
A	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
A	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
A	ASN96

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

Chain	Residue	Details
A	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
A	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
A	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

site_id	CSA6
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j