SAXSdb — 5q0f

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1. Protein Identity and Related Structures Protein Identity & Related Structures

Coagulation factor XI

Homo sapiens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	MET-ASP-ASP-ASP-ASP-LYS-MET-ASP-ASN-GLU-CYS-THR-THR-LYS-ILE-LYS-PRO-ARG × 1 ;methyl [(4R,5E,8S)-8-({(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl}amino)-4-methyl-2-oxo-1,3,4,7,8,10-hexahydro-2H-12,9-(azeno)-1,10-benzodiazacyclotetradecin-15-yl]carbamate ; × 1 SULFATE ION × 2 1,2-ETHANEDIOL × 12 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	FA11_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–238； UniProt 388–625

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	5q0f
Deposition date deposition_date	2017-05-01
Structure title title	FACTOR XIA IN COMPLEX WITH THE INHIBITOR methyl [(4R,5E,8S)-8-({(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl}amino)-4-methyl-2-oxo-1,3,4,7,8,10-hexahydro-2H-12,9-(azeno)-1,10-benzodiazacyclotetradecin-15-yl]carbamate
Keywords keywords	HYDROLASE, SERINE PROTEASE, BLOOD COAGULATION FACTOR, PROTEIN INHIBITOR COMPLEX, HYDROLASE-HYDROLASE inhibitor complex; HYDROLASE/HYDROLASE inhibitor
Experimental Method method	X-RAY DIFFRACTION

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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

5q0f__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

5q0f__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

5q0f__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	18.10 Å
Rg (electron density)	16.86 Å
Total Rg	17.99 Å
Atom count	2017
Residues	243
Excluded volume	35308 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`5q0f__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Description description	Coagulation factor XI
Molecular weight formula_weight	27600.3 kDa
EC 编号 ec_number	3.4.21.27
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	2227

IVGGTASVRGEWPWQVTLHTTSPTQRHLCGGSIIGNQWILTAAHCFYGVESPKILRVYSGILNQSEIKEDTSFFGVQEIIIHDQYKMAESGYDIALLKLETTVGYGDSQRPICLPSKGDRNVIYTDCWVTGWGYRKLRDKIQNTLQKAKIPLVTNEECQKRYRGHKITHKMICAGYREGGKDACKGDSGGPLSCKHNEVWHLVGITSWGEGCAQRERPGVYTNVVEYVDWILEKTQAVHHHHHH

Source Source

Source organism organism	Homo sapiens
Common name common_name	Human
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	MET-ASP-ASP-ASP-ASP-LYS-MET-ASP-ASN-GLU-CYS-THR-THR-LYS-ILE-LYS-PRO-ARG
Molecular weight formula_weight	2159.4 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	H

MDDDDKMDNECTTKIKPR

Entity 3 Entity 3 non-polymer

Description description	;methyl [(4R,5E,8S)-8-({(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl}amino)-4-methyl-2-oxo-1,3,4,7,8,10-hexahydro-2H-12,9-(azeno)-1,10-benzodiazacyclotetradecin-15-yl]carbamate ;
Molecular weight formula_weight	602.0 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 5 Entity 5 non-polymer

Description description	1,2-ETHANEDIOL
Molecular weight formula_weight	62.1 kDa
Source method src_method	syn
Copy count entity_count	12

Entity 6 Entity 6 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	193

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6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d5q0fa_
Class class	b — All beta proteins
Fold Fold fold	b.47 — Trypsin-like serine proteases
Superfamily Superfamily superfamily	b.47.1 — Trypsin-like serine proteases
Family Family family	b.47.1.2 — Eukaryotic proteases

CATH v4.4 (1 domains)

Domain ID domain_id	5q0fA02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	10 — Thrombin, subunit H
Homologous superfamily homologous superfamily	10 — Trypsin-like serine proteases

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7. Citations (9)

Macrocyclic inhibitors of Factor XIa: Discovery of alkyl-substituted macrocyclic amide linkers with improved potency.

Bioorg. Med. Chem. Lett. (2017)

PMID: 28687203 · DOI: 10.1016/j.bmcl.2017.06.058 PRIMARY

Structure-Based Design of Macrocyclic Factor XIa Inhibitors: Discovery of the Macrocyclic Amide Linker.

J. Med. Chem. (2017)

PMID: 28085275 · DOI: 10.1021/acs.jmedchem.6b01460

Novel phenylalanine derived diamides as Factor XIa inhibitors.

Bioorg. Med. Chem. Lett. (2016)

PMID: 26704266 · DOI: 10.1016/j.bmcl.2015.11.089

Orally bioavailable pyridine and pyrimidine-based Factor XIa inhibitors: Discovery of the methyl N-phenyl carbamate P2 prime group.

Bioorg. Med. Chem. (2016)

PMID: 27073051 · DOI: 10.1016/j.bmc.2016.03.062

Pyridine and pyridinone-based factor XIa inhibitors.

Bioorg. Med. Chem. Lett. (2015)

PMID: 25592713 · DOI: 10.1016/j.bmcl.2014.12.050

Structure-based design of inhibitors of coagulation factor XIa with novel P1 moieties.

Bioorg. Med. Chem. Lett. (2015)

PMID: 25728130 · DOI: 10.1016/j.bmcl.2015.01.028

;Discovery of a Potent Parenterally Administered Factor XIa Inhibitor with Hydroxyquinolin-2(1H)-one as the P2' Moiety. ;

ACS Med Chem Lett (2015)

PMID: 26005539 · DOI: 10.1021/acsmedchemlett.5b00066

Tetrahydroquinoline derivatives as potent and selective factor XIa inhibitors.

J. Med. Chem. (2014)

PMID: 24405333 · DOI: 10.1021/jm401670x

Phenylimidazoles as potent and selective inhibitors of coagulation factor XIa with in vivo antithrombotic activity.

J. Med. Chem. (2014)

PMID: 25405503 · DOI: 10.1021/jm5010607

Unit-cell length a length_a	78.600 Å
Unit-cell length b length_b	78.600 Å
Unit-cell length c length_c	106.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	6

Space group space_group	P 32 2 1
Space-group number int_tables_number	154
Crystal system crystal_system	—

Resolution resolution	2.120 Å
Low-resolution limit resolution_low	34.030 Å
R factor r_factor	0.1860
R_work r_work	0.1850
R_free r_free	0.1970

FACTOR XIA IN COMPLEX WITH THE INHIBITOR methyl [(4R,5E,8S)-8-({(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl}amino)-4-methyl-2-oxo-1,3,4,7,8,10-hexahydro-2H-12,9-(azeno)-1,10-benzodiazacyclotetradecin-15-yl]carbamate

1. Protein Identity and Related Structures Protein Identity & Related Structures

Coagulation factor XI

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

5q0f__assembly_1__model_1

5q0f__assembly_1__model_1 | I(q)

5q0f__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 water

6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

7. Citations (9)

FACTOR XIA IN COMPLEX WITH THE INHIBITOR methyl [(4R,5E,8S)-8-({(2E)-3-[5-chloro-2-(1H-tetrazol-1-yl)phenyl]prop-2-enoyl}amino)-4-methyl-2-oxo-1,3,4,7,8,10-hexahydro-2H-12,9-(azeno)-1,10-benzodiazacyclotetradecin-15-yl]carbamate

1. Protein Identity and Related Structures Protein Identity & Related Structures

Coagulation factor XI

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

5q0f__assembly_1__model_1

5q0f__assembly_1__model_1 | I(q)

5q0f__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 water

6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

7. Citations (9)