2A45

Crystal structure of the complex between thrombin and the central "E" region of fibrin

Replaces:  1QVH

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	0005509	molecular_function	calcium ion binding
B	0006508	biological_process	proteolysis
B	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
E	0004252	molecular_function	serine-type endopeptidase activity
E	0005509	molecular_function	calcium ion binding
E	0006508	biological_process	proteolysis
E	0007596	biological_process	blood coagulation
G	0005102	molecular_function	signaling receptor binding
G	0005577	cellular_component	fibrinogen complex
G	0007596	biological_process	blood coagulation
G	0030168	biological_process	platelet activation
G	0051258	biological_process	protein polymerization
H	0005102	molecular_function	signaling receptor binding
H	0005577	cellular_component	fibrinogen complex
H	0030168	biological_process	platelet activation
H	0051258	biological_process	protein polymerization
I	0005102	molecular_function	signaling receptor binding
I	0005577	cellular_component	fibrinogen complex
I	0030168	biological_process	platelet activation
I	0051258	biological_process	protein polymerization
J	0005102	molecular_function	signaling receptor binding
J	0005577	cellular_component	fibrinogen complex
J	0007596	biological_process	blood coagulation
J	0030168	biological_process	platelet activation
J	0051258	biological_process	protein polymerization
K	0005102	molecular_function	signaling receptor binding
K	0005577	cellular_component	fibrinogen complex
K	0030168	biological_process	platelet activation
K	0051258	biological_process	protein polymerization
L	0005102	molecular_function	signaling receptor binding
L	0005577	cellular_component	fibrinogen complex
L	0030168	biological_process	platelet activation
L	0051258	biological_process	protein polymerization

Functional Information from PDB Data

site_id	AC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE 0G6 B 1

Chain	Residue
B	CYS42
B	GLU192
B	GLY193
B	SER195
B	SER214
B	TRP215
B	GLY216
B	GLY226
B	HIS57
B	CYS58
B	TRP60
B	ASN98
B	LEU99
B	ASP189
B	ALA190
B	CYS191

---

site_id	AC2
Number of Residues	17
Details	BINDING SITE FOR RESIDUE 0G6 E 1

Chain	Residue
E	PO42
E	HIS57
E	CYS58
E	TYR60
E	ASN98
E	LEU99
E	ILE174
E	ALA190
E	CYS191
E	GLU192
E	GLY193
E	SER195
E	SER214
E	TRP215
E	GLY216
E	GLY219
E	CYS220

---

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 B 248

Chain	Residue
B	LEU41
B	GLY193
D	ARG15

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 E 2

Chain	Residue
E	0G61
E	LEU41
E	CYS42
E	CYS58
E	LYS60

---

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
B	LEU53-CYS58

---

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

Chain	Residue	Details
B	ASP189-VAL200

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	MOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039

Chain	Residue	Details
I	SER42
L	SER42
B	SER195
E	HIS57
E	ASP102
E	SER195

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569

Chain	Residue	Details
G	SER31
J	SER31

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039

Chain	Residue	Details
G	SER37
J	SER37

---

Catalytic Information from CSA

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

Chain	Residue	Details
B	ASP102
B	SER195
B	GLY193
B	HIS57

---

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

Chain	Residue	Details
E	ASP102
E	SER195
E	GLY193
E	HIS57

---

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

Chain	Residue	Details
B	ASP102
B	SER195
B	HIS57
B	GLY196

---

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

Chain	Residue	Details
E	ASP102
E	SER195
E	HIS57
E	GLY196

---

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

Chain	Residue	Details
B	ASP102
B	SER195
B	HIS57

---

site_id	CSA6
Number of Residues	3
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
E	ASP102
E	SER195
E	HIS57

---