1GGU

HUMAN FACTOR XIII WITH CALCIUM BOUND IN THE ION SITE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003810	molecular_function	protein-glutamine gamma-glutamyltransferase activity
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005737	cellular_component	cytoplasm
A	0007596	biological_process	blood coagulation
A	0018149	biological_process	peptide cross-linking
A	0031012	cellular_component	extracellular matrix
A	0031093	cellular_component	platelet alpha granule lumen
A	0072378	biological_process	blood coagulation, fibrin clot formation
A	0072562	cellular_component	blood microparticle
B	0003810	molecular_function	protein-glutamine gamma-glutamyltransferase activity
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005737	cellular_component	cytoplasm
B	0007596	biological_process	blood coagulation
B	0018149	biological_process	peptide cross-linking
B	0031012	cellular_component	extracellular matrix
B	0031093	cellular_component	platelet alpha granule lumen
B	0072378	biological_process	blood coagulation, fibrin clot formation
B	0072562	cellular_component	blood microparticle

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA A 2001

Chain	Residue
A	ALA457
A	HOH6155
A	HOH6437
A	HOH6438

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA B 2002

Chain	Residue
B	ALA457
B	HOH6135
B	HOH6136
B	HOH6151
B	HOH6293

---

site_id	CAT
Number of Residues	3
Details	CATALYTIC TRIAD IN CHAIN A

Chain	Residue
A	CYS314
A	HIS373
A	ASP396

---

site_id	CBT
Number of Residues	3
Details	CATALYTIC TRIAD IN CHAIN B

Chain	Residue
B	CYS314
B	HIS373
B	ASP396

---

site_id	INA
Number of Residues	4
Details	ION BINDING SITE A - CALCIUM LIGANDS

Chain	Residue
A	GLU490
A	ALA457
A	ASN436
A	GLU485

---

site_id	INB
Number of Residues	4
Details	ION BINDING SITE B - CALCIUM LIGANDS

Chain	Residue
B	ALA457
B	ASN436
B	GLU485
B	GLU490

---

Functional Information from PROSITE/UniProt

site_id	PS00547
Number of Residues	18
Details	TRANSGLUTAMINASES Transglutaminases active site. GQCWVfAGVfnTfLRCLG

Chain	Residue	Details
A	GLY312-GLY329

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Active site: {"evidences":[{"source":"PubMed","id":"7913750","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9988734","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1g0d

Chain	Residue	Details
A	CYS314
A	ASP396
A	HIS373
A	TYR560

---

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1g0d

Chain	Residue	Details
B	CYS314
B	ASP396
B	HIS373
B	TYR560

---

site_id	MCSA1
Number of Residues	5
Details	M-CSA 149

Chain	Residue	Details
A	TRP279	electrostatic stabiliser, hydrogen bond donor
A	CYS314	electrostatic stabiliser
A	HIS373	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	ASP396	electrostatic stabiliser, hydrogen bond acceptor
A	TYR560	electrostatic stabiliser, hydrogen bond donor

---

site_id	MCSA2
Number of Residues	5
Details	M-CSA 149

Chain	Residue	Details
B	TRP279	electrostatic stabiliser, hydrogen bond donor
B	CYS314	electrostatic stabiliser
B	HIS373	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	ASP396	electrostatic stabiliser, hydrogen bond acceptor
B	TYR560	electrostatic stabiliser, hydrogen bond donor

---