5TKS: Factor xia

Factor xia in complex with the inhibitor ((15S)-18-chloro- 15-(((2E)-3-(5-chloro-2-(1H-tetrazol-1-yl)phenyl)-2- propenoyl)amino)-17,19-DIAZATRICYCLO[14.2.1.0~2,7~]NONADECA-1(18),2,4,6,16(19)-pentaen-5-yl)carbamate. Determined by X-ray diffraction at 1.55 Å resolution. Released 1 Mar 2017.

Method: X-ray diffraction
Resolution: 1.55 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,271
Mol. weight: 29.24 kDa
Ligands: 7DL
Released: 1 Mar 2017

Explore 5TKS in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5TKS contains 13 α-helices and 21 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 13 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	17	1	1
β-strand	20-21	2	2
α-helix	22-23	2
β-strand	30-35	6	3
β-strand	39-48	10	3
β-strand	51-54	4	3
α-helix	56-58A	4
α-helix	63-65	3
β-strand	65A-67	4	3
β-strand	72	1	4
α-helix	73-75	3
β-strand	83-90	8	3
α-helix	97-99	3
β-strand	104-108	5	3
α-helix	111-114	4
β-strand	115	1	5
β-strand	118	1	5
α-helix	120-121	2
β-strand	122	1	2
α-helix	123-125	3
α-helix	126-128	3
β-strand	136-140	5	2
β-strand	154	1	4
α-helix	155	1
β-strand	156-159	4	2
β-strand	162-163	2	2
α-helix	165-170	7
β-strand	180-183	4	2
β-strand	189	1	1
β-strand	198-203	6	2
β-strand	206-215	10	2
β-strand	226-230	5	2
α-helix	231-234	4
α-helix	235-242	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Coagulation factor XI	A	protein	244	Homo sapiens	P03951 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>5TKS_1 Coagulation factor XI (chains A)
IVGGTASVRGEWPWQVTLHTTSPTQRHLCGGSIIGNQWILTAAHCFYGVESPKILRVYSG
ILNQSEIKEDTSFFGVQEIIIHDQYKMAESGYDIALLKLETTVGYGDSQRPICLPSKGDR
NVIYTDCWVTGWGYRKLRDKIQNTLQKAKIPLVTNEECQKRYRGHKITHKMICAGYREGG
KDACKGDSGGPLSCKHNEVWHLVGITSWGEGCAQRERPGVYTNVVEYVDWILEKTQAVHH
HHHH

Ligands and cofactors

ID	Name	Formula	Copies
7DL	((15S)-18-chloro- 15-(((2E)-3-(5-chloro-2-(1H-tetrazol-1-yl)phenyl)-2-…	C29 H30 Cl2 N8 O3	1

Water and common crystallization additives (EDO, SO4) are not listed.

Primary citation

Structure-Based Design of Macrocyclic Factor XIa Inhibitors: Discovery of the Macrocyclic Amide Linker. Corte, J.R., Fang, T., Osuna, H. et al. J Med Chem (2017) 60:1060-1075. DOI 10.1021/acs.jmedchem.6b01460 · PubMed

Other PDB entries of the same protein (UniProt P03951 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7MBO 0.92 Å, FACTOR XIA (PICHIA PASTORIS; C500S [C122S]) IN COMPLEX WITH THE INHIBITOR Milvexian…
6TS4 1.17 Å, Coagulation factor XI protease domain in complex with active site inhibitor
4CRG 1.25 Å, Creating novel F1 inhibitors through fragment based lead generation and structure aided…
8BO6 1.25 Å, Coagulation factor XI protease domain in complex with active site inhibitor 2
8BO7 1.25 Å, Coagulation factor XI protease domain in complex with active site inhibitor 34
6USY 1.26 Å, Coagulation factor XI catalytic domain (C123S) in complex with nvp-XIV936
6TS5 1.29 Å, Coagulation factor XI protease domain in complex with active site inhibitor
6TS6 1.33 Å, Coagulation factor XI protease domain in complex with active site inhibitor
7V11 1.47 Å, Factor XIa in Complex with Compound 2e
5EXN 1.49 Å, FACTOR XIA (C500S [C122S]) IN COMPLEX WITH THE INHIBITOR methyl…
7V16 1.5 Å, Factor XIa in Complex with Compound 2j
7V17 1.52 Å, Factor XIa in Complex with Compound 2k

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