1DX5

Crystal structure of the thrombin-thrombomodulin complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004252	molecular_function	serine-type endopeptidase activity
A	0005576	cellular_component	extracellular region
A	0006508	biological_process	proteolysis
A	0007596	biological_process	blood coagulation
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	0005576	cellular_component	extracellular region
C	0006508	biological_process	proteolysis
C	0007596	biological_process	blood coagulation
D	0004252	molecular_function	serine-type endopeptidase activity
D	0005576	cellular_component	extracellular region
D	0006508	biological_process	proteolysis
D	0007596	biological_process	blood coagulation
I	0004888	molecular_function	transmembrane signaling receptor activity
I	0005509	molecular_function	calcium ion binding
I	0016020	cellular_component	membrane
J	0004888	molecular_function	transmembrane signaling receptor activity
J	0005509	molecular_function	calcium ion binding
J	0016020	cellular_component	membrane
K	0004888	molecular_function	transmembrane signaling receptor activity
K	0005509	molecular_function	calcium ion binding
K	0016020	cellular_component	membrane
L	0004888	molecular_function	transmembrane signaling receptor activity
L	0005509	molecular_function	calcium ion binding
L	0016020	cellular_component	membrane
M	0004252	molecular_function	serine-type endopeptidase activity
M	0005509	molecular_function	calcium ion binding
M	0006508	biological_process	proteolysis
M	0007596	biological_process	blood coagulation
N	0004252	molecular_function	serine-type endopeptidase activity
N	0005509	molecular_function	calcium ion binding
N	0006508	biological_process	proteolysis
N	0007596	biological_process	blood coagulation
O	0004252	molecular_function	serine-type endopeptidase activity
O	0005509	molecular_function	calcium ion binding
O	0006508	biological_process	proteolysis
O	0007596	biological_process	blood coagulation
P	0004252	molecular_function	serine-type endopeptidase activity
P	0005509	molecular_function	calcium ion binding
P	0006508	biological_process	proteolysis
P	0007596	biological_process	blood coagulation

Functional Information from PROSITE/UniProt

site_id	PS00010
Number of Residues	12
Details	ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. ChNlpgtFeCiC

Chain	Residue	Details
I	CYS437-CYS448

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

Chain	Residue	Details
M	LEU53-CYS58

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

Chain	Residue	Details
M	ASP189-VAL200

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site_id	PS01186
Number of Residues	15
Details	EGF_2 EGF-like domain signature 2. CeCpeGYilddgfi.C

Chain	Residue	Details
I	CYS407-CYS421

---

site_id	PS01187
Number of Residues	24
Details	EGF_CA Calcium-binding EGF-like domain signature. DiDECenggf.........Csgv....ChNlpgtFeC

Chain	Residue	Details
I	ASP423-CYS446

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	ACT_SITE: Charge relay system

Chain	Residue	Details
M	HIS57
P	HIS57
P	ASP102
P	SER195
M	ASP102
M	SER195
N	HIS57
N	ASP102
N	SER195
O	HIS57
O	ASP102
O	SER195

---

site_id	SWS_FT_FI2
Number of Residues	4
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
M	ASN60
N	ASN60
O	ASN60
P	ASN60

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
M	ASP102
M	SER195
M	GLY193
M	HIS57

---

site_id	CSA10
Number of Residues	3
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
N	ASP102
N	SER195
N	HIS57

---

site_id	CSA11
Number of Residues	3
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
O	ASP102
O	SER195
O	HIS57

---

site_id	CSA12
Number of Residues	3
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
P	ASP102
P	SER195
P	HIS57

---

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
N	ASP102
N	SER195
N	GLY193
N	HIS57

---

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
O	ASP102
O	SER195
O	GLY193
O	HIS57

---

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

Chain	Residue	Details
P	ASP102
P	SER195
P	GLY193
P	HIS57

---

site_id	CSA5
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
M	ASP102
M	SER195
M	HIS57
M	GLY196

---

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

Chain	Residue	Details
N	ASP102
N	SER195
N	HIS57
N	GLY196

---

site_id	CSA7
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
O	ASP102
O	SER195
O	HIS57
O	GLY196

---

site_id	CSA8
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
P	ASP102
P	SER195
P	HIS57
P	GLY196

---

site_id	CSA9
Number of Residues	3
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
M	ASP102
M	SER195
M	HIS57

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