7KVE: Human Factor V

Cryo-EM structure of human Factor V at 3.3 Angstrom resolution. Determined by electron microscopy at 3.3 Å resolution. Released 10 Mar 2021.

Method: Electron microscopy
Resolution: 3.3 Å
Organism: Homo sapiens
Chains: 1
Atoms: 11,142
Mol. weight: 248.97 kDa
Released: 10 Mar 2021

Explore 7KVE in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7KVE contains 24 α-helices and 113 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 B: 24 helices, 113 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	1
β-strand	8-12	5	2
α-helix	24-27	4
β-strand	36-40	5	2
β-strand	41	1	3
α-helix	43-45	3
β-strand	48	1	3
β-strand	62-64	3	4
β-strand	69-73	5	1
β-strand	75-76	2	2
β-strand	82	1	5
β-strand	85	1	4
β-strand	114	1	5
α-helix	115	1
β-strand	118-119	2	2
β-strand	122-125	4	1
β-strand	139	1	6
β-strand	142-145	4	4
β-strand	159-164	6	4
β-strand	165	1	6
β-strand	185-189	5	7
α-helix	192-194	3
β-strand	206	1	7
β-strand	209	1	7
α-helix	215-216	2
β-strand	217-219	3	8
β-strand	224-233	10	7
β-strand	238-240	3	9
β-strand	241-243	3	10
β-strand	249	1	7
β-strand	250	1	11
β-strand	253	1	11
β-strand	259-261	3	9
β-strand	266-271	6	7
β-strand	278-279	2	8
β-strand	280-282	3	10
β-strand	295-298	4	8
β-strand	324-328	5	12
β-strand	329	1	13
α-helix	345-351	7
β-strand	367	1	13
β-strand	370-371	2	12
β-strand	379	1	12
β-strand	394-397	4	14
β-strand	405-409	5	12
β-strand	415	1	15
β-strand	418-419	2	14
α-helix	423-425	3
β-strand	447	1	15
β-strand	453-454	2	12
α-helix	464-466	3
β-strand	473-478	6	14
α-helix	483-489	7
β-strand	492-497	6	14
β-strand	515-520	6	16
β-strand	522-524	3	17
α-helix	525-527	3
α-helix	532-536	5
α-helix	550-555	6
β-strand	557-559	3	17
β-strand	579-586	8	16
β-strand	594-597	4	18
β-strand	603	1	16
β-strand	605	1	19
β-strand	608	1	19
β-strand	612-615	4	18
α-helix	616	1
β-strand	621-626	6	16
β-strand	633	1	20
β-strand	636-637	2	18
β-strand	648	1	18
β-strand	651	1	20
β-strand	1550-1554	5	21
β-strand	1556-1563	8	22
β-strand	1566	1	23
α-helix	1568-1570	3
β-strand	1587-1594	8	22
β-strand	1595	1	24
β-strand	1603	1	24
α-helix	1609-1611	3
β-strand	1620	1	25
β-strand	1623	1	26
β-strand	1626-1632	7	21
β-strand	1634	1	22
β-strand	1640	1	27
β-strand	1648	1	21
α-helix	1651-1653	3
α-helix	1666-1668	3
β-strand	1672	1	27
β-strand	1678-1683	6	21
α-helix	1686-1688	3
β-strand	1697-1698	2	26
β-strand	1701-1703	3	28
α-helix	1708-1712	5
β-strand	1717-1719	3	28
β-strand	1720	1	25
β-strand	1722-1723	2	26
β-strand	1740-1744	5	29
β-strand	1745-1749	5	30
α-helix	1769-1771	3
β-strand	1776-1780	5	30
β-strand	1784	1	23
β-strand	1791-1792	2	31
β-strand	1799-1803	5	29
β-strand	1812-1816	5	32
β-strand	1834-1836	3	32
β-strand	1841-1845	5	29
β-strand	1852-1853	2	31
β-strand	1856-1858	3	32
α-helix	1861-1864	4
β-strand	1869-1870	2	32
β-strand	1873-1874	2	31
β-strand	1881-1882	2	33
α-helix	1892-1894	3
β-strand	1895-1897	3	34
α-helix	1906-1908	3
β-strand	1910	1	35
β-strand	1935-1937	3	34
β-strand	1943-1950	8	33
β-strand	1962-1970	9	34
β-strand	2000-2010	11	33
β-strand	2012-2020	9	34
β-strand	2028	1	35
β-strand	2030-2032	3	33
β-strand	2040-2041	2	36
α-helix	2051-2053	3
β-strand	2054-2056	3	36
β-strand	2061	1	37
β-strand	2067	1	37
β-strand	2095-2110	16	36
β-strand	2112-2113	2	36
β-strand	2120-2129	10	36
β-strand	2137-2138	2	36
β-strand	2140	1	38
β-strand	2147	1	38
β-strand	2160-2181	22	36
β-strand	2189-2193	5	36

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Coagulation factor V	B	protein	2196	Homo sapiens	P12259 (AlphaFold model)

Sequence of entity 1 (B), FASTA

>7KVE_1 Coagulation factor V (chains B)
AQLRQFYVAAQGISWSYRPEPTNSSLNLSVTSFKKIVYREYEPYFKKEKPQSTISGLLGP
TLYAEVGDIIKVHFKNKADKPLSIHPQGIRYSKLSEGASYLDHTFPAEKMDDAVAPGREY
TYEWSISEDSGPTHDDPPCLTHIYYSHENLIEDFNSGLIGPLLICKKGTLTEGGTQKTFD
KQIVLLFAVFDESKSWSQSSSLMYTVNGYVNGTMPDITVCAHDHISWHLLGMSSGPELFS
IHFNGQVLEQNHHKVSAITLVSATSTTANMTVGPEGKWIISSLTPKHLQAGMQAYIDIKN
CPKKTRNLKKITREQRRHMKRWEYFIAAEEVIWDYAPVIPANMDKKYRSQHLDNFSNQIG
KHYKKVMYTQYEDESFTKHTVNPNMKEDGILGPIIRAQVRDTLKIVFKNMASRPYSIYPH
GVTFSPYEDEVNSSFTSGRNNTMIRAVQPGETYTYKWNILEFDEPTENDAQCLTRPYYSD
VDIMRDIASGLIGLLLICKSRSLDRRGIQRAADIEQQAVFAVFDENKSWYLEDNINKFCE
NPDEVKRDDPKFYESNIMSTINGYVPESITTLGFCFDDTVQWHFCSVGTQNEILTIHFTG
HSFIYGKRHEDTLTLFPMRGESVTVTMDNVGTWMLTSMNSSPRSKKLRLKFRDVKCIPDD
DEDSYEIFEPPESTVMATRKMHDRLEPEDEESDADYDYQNRLAAALGIRSFRNSSLNQEE
EEFNLTALALENGTEFVSSNTDIIVGSNYSSPSNISKFTVNNLAEPQKAPSHQQATTAGS
PLRHLIGKNSVLNSSTAEHSSPYSEDPIEDPLQPDVTGIRLLSLGAGEFKSQEHAKHKGP
KVERDQAAKHRFSWMKLLAHKVGRHLSQDTGSPSGMRPWEDLPSQDTGSPSRMRPWKDPP
SDLLLLKQSNSSKILVGRWHLASEKGSYEIIQDTDEDTAVNNWLISPQNASRAWGESTPL
ANKPGKQSGHPKFPRVRHKSLQVRQDGGKSRLKKSQFLIKTRKKKKEKHTHHAPLSPRTF
HPLRSEAYNTFSERRLKHSLVLHKSNETSLPTDLNQTLPSMDFGWIASLPDHNQNSSNDT
GQASCPPGLYQTVPPEEHYQTFPIQDPDQMHSTSDPSHRSSSPELSEMLEYDRSHKSFPT
DISQMSPSSEHEVWQTVISPDLSQVTLSPELSQTNLSPDLSHTTLSPELIQRNLSPALGQ
MPISPDLSHTTLSPDLSHTTLSLDLSQTNLSPELSQTNLSPALGQMPLSPDLSHTTLSLD
FSQTNLSPELSHMTLSPELSQTNLSPALGQMPISPDLSHTTLSLDFSQTNLSPELSQTNL
SPALGQMPLSPDPSHTTLSLDLSQTNLSPELSQTNLSPDLSEMPLFADLSQIPLTPDLDQ
MTLSPDLGETDLSPNFGQMSLSPDLSQVTLSPDISDTTLLPDLSQISPPPDLDQIFYPSE
SSQSLLLQEFNESFPYPDLGQMPSPSSPTLNDTFLSKEFNPLVIVGLSKDGTDYIEIIPK
EEVQSSEDDYAEIDYVPYDDPYKTDVRTNINSSRDPDNIAAWYLRSNNGNRRNYYIAAEE
ISWDYSEFVQRETDIEDSDDIPEDTTYKKVVFRKYLDSTFTKRDPRGEYEEHLGILGPII
RAEVDDVIQVRFKNLASRPYSLHAHGLSYEKSSEGKTYEDDSPEWFKEDNAVQPNSSYTY
VWHATERSGPESPGSACRAWAYYSAVNPEKDIHSGLIGPLLICQKGILHKDSNMPMDMRE
FVLLFMTFDEKKSWYYEKKSRSSWRLTSSEMKKSHEFHAINGMIYSLPGLKMYEQEWVRL
HLLNIGGSQDIHVVHFHGQTLLENGNKQHQLGVWPLLPGSFKTLEMKASKPGWWLLNTEV
GENQRAGMQTPFLIMDRDCRMPMGLSTGIISDSQIKASEFLGYWEPRLARLNNGGSYNAW
SVEKLAAEFASKPWIQVDMQKEVIITGIQTQGAKHYLKSCYTTEFYVAYSSNQINWQIFK
GNSTRNVMYFNGNSDASTIKENQFDPPIVARYIRISPTRAYNRPTLRLELQGCEVNGCST
PLGMENGKIENKQITASSFKKSWWGDYWEPFRARLNAQGRVNAWQAKANNNKQWLEIDLL
KIKKITAIITQGCKSLSSEMYVKSYTIHYSEQGVEWKPYRLKSSMVDKIFEGNTNTKGHV
KNFFNPPIISRFIRVIPKTWNQSIALRLELFGCDIY

Primary citation

Cryo-EM structures of human coagulation factors V and Va. Ruben, E.A., Rau, M.J., Fitzpatrick, J.A.J. et al. Blood (2021) 137:3137-3144. DOI 10.1182/blood.2021010684 · 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…
36JB 2.9 Å, Coagulation factor V DTQQ, membrane-bound, on Ptd-choline : Ptd-serine 75:25 vesicles
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

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