36JB: Coagulation factor V

Coagulation factor V DTQQ, membrane-bound, on Ptd-choline : Ptd-serine 75:25 vesicles. Determined by electron microscopy at 2.9 Å resolution. Released 16 Sept 2026.

Method: Electron microscopy
Resolution: 2.9 Å
Organism: Homo sapiens
Chains: 1
Atoms: 10,077
Mol. weight: 176.25 kDa
Ligands: NAG, SEP, CU1, CA
Released: 16 Sept 2026

Explore 36JB in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

36JB contains 28 α-helices and 107 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: 28 helices, 107 β-strands

Element	Residues	Length	Sheet
β-strand	3-6	4	1
β-strand	8-15	8	1
β-strand	33-40	8	1
β-strand	41	1	2
α-helix	43-45	3
β-strand	48	1	2
β-strand	62-65	4	3
β-strand	69-76	8	1
β-strand	82	1	4
β-strand	85-86	2	3
α-helix	106-109	4
β-strand	114	1	4
α-helix	115	1
β-strand	119-125	7	1
β-strand	139-145	7	3
α-helix	150-155	6
β-strand	160-165	6	3
β-strand	170	1	5
β-strand	176	1	5
β-strand	181-191	11	6
β-strand	202-206	5	6
β-strand	209-210	2	6
α-helix	215-216	2
β-strand	217-220	4	7
β-strand	224-232	9	6
β-strand	238-243	6	7
β-strand	248-249	2	6
β-strand	254-255	2	6
β-strand	258-261	4	7
β-strand	264-271	8	6
β-strand	276-282	7	7
α-helix	285-289	5
β-strand	293-299	7	7
β-strand	322-334	13	8
β-strand	362-371	10	8
β-strand	379	1	8
α-helix	385-388	4
β-strand	395-398	4	9
β-strand	402-409	8	8
β-strand	415	1	10
β-strand	418-419	2	9
β-strand	447	1	10
α-helix	448	1
β-strand	452-458	7	8
α-helix	461-463	3
α-helix	465-466	2
β-strand	472-478	7	9
α-helix	483-489	7
β-strand	493-498	6	9
β-strand	514-524	11	11
α-helix	531-535	5
α-helix	550-555	6
β-strand	557-561	5	11
β-strand	564	1	11
α-helix	566-568	3
β-strand	572-575	4	12
β-strand	578-588	11	11
β-strand	594-598	5	12
β-strand	603-605	3	11
β-strand	608-610	3	11
β-strand	612-615	4	12
β-strand	621-627	7	11
β-strand	631-637	7	12
β-strand	649-654	6	12
α-helix	1536-1543	8
β-strand	1551-1564	14	13
β-strand	1586-1594	9	13
β-strand	1595	1	14
β-strand	1603	1	14
α-helix	1611-1613	3
β-strand	1620-1623	4	15
β-strand	1627-1635	9	13
β-strand	1640	1	16
β-strand	1643-1644	2	15
β-strand	1648	1	13
α-helix	1664-1666	3
β-strand	1672	1	16
β-strand	1677-1683	7	13
α-helix	1686-1688	3
α-helix	1691	1
β-strand	1697-1703	7	15
α-helix	1708-1713	6
β-strand	1717-1723	7	15
β-strand	1728	1	17
β-strand	1735	1	17
β-strand	1739-1744	6	18
β-strand	1745-1749	5	19
α-helix	1750-1752	3
β-strand	1776-1780	5	19
β-strand	1783	1	19
β-strand	1791-1793	3	20
β-strand	1797-1804	8	18
β-strand	1812-1816	5	20
β-strand	1821-1823	3	18
β-strand	1829-1831	3	18
β-strand	1833-1836	4	20
β-strand	1840-1847	8	18
β-strand	1852-1858	7	20
α-helix	1861-1866	6
β-strand	1869-1875	7	20
α-helix	1876	1
β-strand	1881-1882	2	21
α-helix	1892-1894	3
β-strand	1895-1897	3	21
α-helix	1906-1908	3
β-strand	1920-1921	2	22
β-strand	1935-1951	17	21
β-strand	1953-1955	3	23
β-strand	1958-1960	3	23
β-strand	1962-1970	9	21
β-strand	1977-1978	2	21
β-strand	1990-1991	2	21
α-helix	1999	1
β-strand	2000-2020	21	21
β-strand	2025-2026	2	22
β-strand	2027-2034	8	21
β-strand	2041	1	24
β-strand	2054-2056	3	24
β-strand	2061-2062	2	25
β-strand	2066-2067	2	25
α-helix	2070-2072	3
β-strand	2074	1	24
β-strand	2084-2085	2	26
β-strand	2095-2111	17	24
β-strand	2113-2114	2	27
β-strand	2119-2120	2	27
β-strand	2121-2130	10	24
β-strand	2137-2138	2	24
α-helix	2139	1
β-strand	2140	1	28
β-strand	2147	1	28
β-strand	2150-2151	2	24
β-strand	2160-2181	22	24
β-strand	2185-2186	2	26
β-strand	2187-2193	7	24

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Coagulation factor V	A	protein	1515	Homo sapiens	P12259 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>36JB_1 Coagulation factor V (chains A)
AQLRQFYVAAQGISWSYRPEPTNSSLNLSVTSFKKIVYREYEPYFKKEKPQSTISGLLGP
TLYAEVGDIIKVHFKNKADKPLSIHPQGIRYSKLSEGASYLDHTFPAEKMDDAVAPGREY
TYEWSISEDSGPTHDDPPCLTHIYYSHENLIEDFNSGLIGPLLICKKGTLTEGGTQKTFD
KQIVLLFAVFDESKSWSQSSSLMYTVNGYVNGTMPDITVCAHDHISWHLLGMSSGPELFS
IHFNGQVLEQNHHKVSAITLVSATSTTANMTVGPEGKWIISSLTPKHLQAGMQAYIDIKN
CPKKTRNLKKITREQRRHMKRWEYFIAAEEVIWDYAPVIPANMDKKYRSQHLDNFSNQIG
KHYKKVMYTQYEDESFTKHTVNPNMKEDGILGPIIRAQVRDTLKIVFKNMASRPYSIYPH
GVTFSPYEDEVNSSFTSGRNNTMIRAVQPGETYTYKWNILEFDEPTENDAQCLTRPYYSD
VDIMRDIASGLIGLLLICKSRSLDRRGIQRAADIEQQAVFAVFDENKSWYLEDNINKFCE
NPDEVKRDDPKFYESNIMSTINGYVPESITTLGFCFDDTVQWHFCSVGTQNEILTIHFTG
HSFIYGKRHEDTLTLFPMRGESVTVTMDNVGTWMLTSMNSSPRSKKLRLKFRDVKCIPDD
DEDSYEIFEPPESTVMATRKMHDRLEPEDEESDADYDYQNRLAAALGIQSFRNSSLNQEE
EEFNLTALALENGTEFVSSNTDIIVGSNYSSPSNISKFTVNNLAEPQKAPSHQQATTAGS
PLRHLIGKNSVLNSSTAEHSSPYSEDPIEDTDYIEIIPKEEVQSSEDDYAEIDYVPYDDP
YKTDVRTNINSSRDPDNIAAWYLQSNNGNRRNYYIAAEEISWDYSEFVQRETDIEDSDDI
PEDTTYKKVVFRKYLDSTFTKRDPRGEYEEHLGILGPIIRAEVDDVIQVRFKNLASRPYS
LHAHGLSYEKSSEGKTYEDDSPEWFKEDNAVQPNSSYTYVWHATERSGPESPGSACRAWA
YYSAVNPEKDIHSGLIGPLLICQKGILHKDSNMPVDMREFVLLFMTFDEKKSWYYEKKSR
SSWRLTSSEMKKSHEFHAINGMIYSLPGLKMYEQEWVRLHLLNIGGSQDIHVVHFHGQTL
LENGNKQHQLGVWPLLPGSFKTLEMKASKPGWWLLNTEVGENQRAGMQTPFLIMDRDCRM
PMGLSTGIISDSQIKASEFLGYWEPRLARLNNGGSYNAWSVEKLAAEFASKPWIQVDMQK
EVIITGIQTQGAKHYLKSCYTTEFYVAYSSNQINWQIFKGNSTRNVMYFNGNSDASTIKE
NQFDPPIVARYIRISPTRAYNRPTLRLELQGCEVNGCSTPLGMENGKIENKQITASSFKK
SWWGDYWEPFRARLNAQGRVNAWQAKANNNKQWLEIDLLKIKKITAIITQGCKSLSSEMY
VKSYTIHYSEQGVEWKPYRLKSSMVDKIFEGNTNTKGHVKNFFNPPIISRFIRVIPKTWN
QSITLRLELFGCDIY

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	1
SEP	Phosphoserine	C3 H8 N O6 P	2
CU1	Copper (I) ion	Cu	1
CA	Calcium ion	Ca	2

Primary citation

Structural basis for membrane binding by coagulation factors V and VIII and their specificity for phosphatidylserine-containing membranes. Kolyadko, V.N., Pumroy, R.A., Moiseenkova-Bell, V.Y. et al. Proc Natl Acad Sci U S A (2026) 123:e2622255123-e2622255123. DOI 10.1073/pnas.2622255123 · PubMed

Other PDB entries of the same protein (UniProt P12259 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9I24 1.2 Å, Coagulation factor Xa complex with a2-loop peptide
3P6Z 1.7 Å, Structural basis of thrombin mediated factor V activation: essential role of the…
3S9C 1.8 Å, Russell's viper venom serine proteinase, RVV-V in complex with the fragment (residues…
1CZT 1.87 Å, Crystal structure of the C2 domain of human coagulation factor V
1CZS 1.9 Å, Crystal structure of the C2 domain of human coagulation factor V: complex with…
1CZV 2.4 Å, Crystal structure of the C2 domain of human coagulation factor V: dimeric crystal form
3P70 2.55 Å, Structural basis of thrombin-mediated factor V activation: essential role of the…
9T00 2.8 Å, Crystal structure of prethrombin-2 with a peptide corresponding to the C-terminus of the…
9MOV 3.0 Å, Cryo-EM structure of factor Va bound to activated protein C
8TN9 3.05 Å, Structural architecture of the acidic region of the B domain of coagulation factor V
9TLE 3.1 Å, Structure of human prothrombinase with prothrombin
9TLG 3.1 Å, Structure of human prothrombinase with meizothrombin

Browse structure collections

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