4CRG: Coagulation factor XIa light chain

Creating novel F1 inhibitors through fragment based lead generation and structure aided drug design. Determined by X-ray diffraction at 1.25 Å resolution. Released 11 Feb 2015.

Method: X-ray diffraction
Resolution: 1.25 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,421
Mol. weight: 27.89 kDa
Ligands: J4X
Released: 11 Feb 2015

Explore 4CRG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4CRG contains 12 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: 12 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	37D-46	10	3
β-strand	51-54	4	3
α-helix	56-59	4
α-helix	62-64	3
β-strand	65-68	4	3
β-strand	73	1	4
α-helix	74-76	3
β-strand	83-90	8	3
α-helix	97-99	3
β-strand	104-108	5	3
β-strand	115	1	5
β-strand	118	1	5
α-helix	121-122	2
β-strand	123	1	2
α-helix	124-126	3
α-helix	127-129	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	165-171	7
β-strand	180-183	4	2
β-strand	189	1	1
β-strand	198-202A	6	2
β-strand	202D-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 XIa light chain	A	protein	238	Homo sapiens	P03951 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4CRG_1 Coagulation factor XIa light chain (chains A)
IVGGTASVRGEWPWQVTLHTTSPTQRHLCGGSIIGNQWILTAAHCFYGVESPKILRVYSG
ILNQAEIAEDTSFFGVQEIIIHDQYKMAESGYDIALLKLETTVNYADSQRPISLPSKGDR
NVIYTDCWVTGWGYRKLRDKIQNTLQKAKIPLVTNEECQKRYRGHKITHKMICAGYREGG
KDACKGDSGGPLSCKHNEVWHLVGITSWGEGCAQRERPGVYTNVVEYVDWILEKTQAV

Ligands and cofactors

ID	Name	Formula	Copies
J4X	6-carbamimidoyl-N-phenyl-4-(pyrimidin-2-ylamino)naphthalene-2-carboxamide	C22 H18 N6 O	1

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

Primary citation

Creating Novel Activated Factor Xi Inhibitors Through Fragment Based Lead Generation and Structure Aided Drug Design. Fjellstrom, O., Akkaya, S., Beisel, H. et al. PLoS One (2015) 10:13705. DOI 10.1371/JOURNAL.PONE.0113705 · 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
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
5TKS 1.55 Å, Factor xia in complex with the inhibitor ((15S)-18-chloro-…

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