6R8X

COAGULATION FACTOR XI CATALYTIC DOMAIN IN COMPLEX WITH FAB-PORTION OF MAA868

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
IMGT Antibody Annotation
SAbDab Antibody Annotation
Thera-SAbDab Antibody Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Pharos: Disease Associations

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d6r8xa_	All beta proteins	Trypsin-like serine proteases	Trypsin-like serine proteases	Eukaryotic proteases	Coagulation factor XI	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Trypsin-like serine proteases	8044201	3000114	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Trypsin_1	e6r8xA1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: FMN-binding split barrel 2	F: Trypsin_1	ECOD (1.6)
B	C1-set	e6r8xB1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: C1-set	ECOD (1.6)
B	V-set_3	e6r8xB2	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: V-set_3	ECOD (1.6)
C	C1-set_1	e6r8xC2	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: C1-set_1	ECOD (1.6)
C	V-set_12	e6r8xC1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: V-set_12	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.40.10.10	Mainly Beta	Beta Barrel	Thrombin, subunit H	Trypsin-like serine proteases	CATH (utative)
B	2.60.40.10	Mainly Beta	Sandwich	Immunoglobulin-like	Immunoglobulins	CATH (utative)
C	2.60.40.10	Mainly Beta	Sandwich	Immunoglobulin-like	Immunoglobulins	CATH (utative)

IMGT Antibody Annotation IMGT Database Homepage

Chain	Protein Name	Description	Organism Name	Gene Allele Name(s)	Domain Name(s)	Receptor Type	Receptor Description	Provenance Source
A	Coagulation factor XI, EC: 3.4.21.27	null	Homo sapiens (human)	F11*01	R-LIKE-DOMAIN PEPTIDASE-S1	RPI	PEPTIDASE-S1	IMGT (202452-0)
B	Fab MAA868, anti-Factor-XI	L-LAMBDA	Homo sapiens (human)	IGLV1-4401, IGLJ201, IGLJ301, IGLC201, IGLC202, IGLC304	V-DOMAIN V-LAMBDA, C-DOMAIN C-LAMBDA	IG	FAB-GAMMA-1_KAPPA	IMGT (202452-0)
C	Fab MAA868, anti-Factor-XI	VH-CH1	Homo sapiens (human)	IGHV3-2301, IGHV3-23D01, IGHJ401, IGHJ402, IGHJ403, IGHG103, IGHG108, IGHG106	V-DOMAIN VH, C-DOMAIN CH1	IG	FAB-GAMMA-1_KAPPA	IMGT (202452-0)

SAbDab Antibody Annotation SAbDab Database Homepage

Chain	Chain Class	Chain Subclass	Chain Type	Antigen Name(s)	Provenance Source
B	Light Chain	IGLV1	Lambda	coagulation factor xi	SAbDab (2025-01-03)
C	Heavy Chain	IGHV3	-	coagulation factor xi	SAbDab (2025-01-03)

Thera-SAbDab Antibody Annotation Thera-SAbDab Database Homepage

Chain	Name	Target	Provenance Source
B	Abelacimab	F11	Therapeutic SAbDab (2025-01-03)
C	Abelacimab	F11	Therapeutic SAbDab (2025-01-03)

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Coagulation factor XI	serine-type exopeptidase activity peptidase activity serine-type aminopeptidase activity catalytic activity, acting on a protein serine hydrolase activity serine-type peptidase activity aminopeptidase activity hydrolase activity exopeptidase activity catalytic activity serine-type endopeptidase activity endopeptidase activity heparin binding glycosaminoglycan binding serine-type exopeptidase activity peptidase activity serine-type aminopeptidase activity catalytic activity, acting on a protein serine hydrolase activity serine-type peptidase activity aminopeptidase activity hydrolase activity exopeptidase activity catalytic activity serine-type endopeptidase activity endopeptidase activity heparin binding glycosaminoglycan binding binding carbohydrate derivative binding sulfur compound binding identical protein binding protein binding	multicellular organismal process regulation of body fluid levels wound healing response to stimulus hemostasis biological regulation blood coagulation response to stress coagulation regulation of biological quality response to wounding regulation of response to external stimulus negative regulation of biological process positive regulation of biological process multicellular organismal process regulation of body fluid levels wound healing response to stimulus hemostasis biological regulation blood coagulation response to stress coagulation regulation of biological quality response to wounding regulation of response to external stimulus negative regulation of biological process positive regulation of biological process regulation of coagulation regulation of response to wounding regulation of response to stress regulation of multicellular organismal process regulation of hemostasis regulation of biological process negative regulation of response to stimulus regulation of blood coagulation negative regulation of wound healing negative regulation of blood coagulation response to external stimulus negative regulation of response to wounding positive regulation of fibrinolysis negative regulation of hemostasis fibrinolysis regulation of fibrinolysis negative regulation of coagulation regulation of response to stimulus negative regulation of response to external stimulus regulation of wound healing negative regulation of multicellular organismal process zymogen activation primary metabolic process gene expression macromolecule biosynthetic process protein maturation biosynthetic process proteolysis protein processing metabolic process cellular process protein metabolic process macromolecule metabolic process plasminogen activation	cellular anatomical structure membrane extracellular region extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle organelle extracellular space vesicle extracellular membrane-bounded organelle cell periphery plasma membrane
B	anti-Factor-XI Fab fragment light chain MAA868	-	-	-
C	anti-Factor-XI Fab fragment heavy chain MAA868	-	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR000177	Apple domain	Domain
A	IPR009003	Peptidase S1, PA clan	Homologous Superfamily
A	IPR001314	Peptidase S1A, chymotrypsin family	Family
A	IPR033116	Serine proteases, trypsin family, serine active site	Active Site
A	IPR001254	Serine proteases, trypsin domain	Domain
A	IPR003609	PAN/Apple domain	Domain
A	IPR043504	Peptidase S1, PA clan, chymotrypsin-like fold	Homologous Superfamily
A	IPR018114	Serine proteases, trypsin family, histidine active site	Active Site

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A	Pharos: P03951	congenital factor XI deficiency hypertensive disorder cerebrovascular disorder lung carcinoma pancreatic ductal adenocarcinoma pancreatic intraductal papillary-mucinous neoplasm with low grade dysplasia lung adenocarcinoma malignant pancreatic neoplasm pancreatic intraductal papillary-mucinous carcinoma thrombotic disease factor XI deficiency lung cancer non-small cell lung carcinoma pancreatic intraductal papillary-mucinous neoplasm vascular disease

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.