6MF0: Coagulation factor VIII chimera

Crystal Structure Determination of Human/Porcine Chimera Coagulation Factor VIII. Determined by X-ray diffraction at 3.2 Å resolution. Released 11 Sept 2019.

Method: X-ray diffraction
Resolution: 3.2 Å
Organisms: Sus scrofa, Homo sapiens
Chains: 2
Atoms: 20,622
Mol. weight: 342.56 kDa
Ligands: CU1, ZN, CA
Released: 11 Sept 2019

Explore 6MF0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6MF0 contains 48 α-helices and 239 β-strands across 2 chains. 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: 25 helices, 116 β-strands

Element	Residues	Length	Sheet
β-strand	2-5	4	1
β-strand	8-14	7	2
α-helix	21-23	3
β-strand	47-53	7	2
β-strand	55	1	3
β-strand	63	1	3
α-helix	64-65	2
α-helix	73	1
β-strand	74-80	7	4
β-strand	84-87	4	1
β-strand	88	1	5
β-strand	90-92	3	2
β-strand	97	1	6
β-strand	100-101	2	4
α-helix	122-124	3
β-strand	129	1	6
β-strand	132	1	2
β-strand	136	1	5
β-strand	139	1	1
α-helix	143-145	3
β-strand	154-160	7	4
α-helix	165-169	5
β-strand	174-180	7	4
β-strand	193-201	9	7
β-strand	202-204	3	8
α-helix	205-207	3
β-strand	231-233	3	8
β-strand	235	1	9
β-strand	238	1	9
β-strand	241	1	10
β-strand	247-249	3	10
β-strand	253-261	9	7
β-strand	268-272	5	10
β-strand	277-279	3	7
β-strand	282-284	3	7
β-strand	287-289	3	10
β-strand	294-300	7	7
β-strand	305-311	7	10
β-strand	322-328	7	10
α-helix	378-380	3
β-strand	381-394	14	11
α-helix	408-411	4
β-strand	415	1	12
β-strand	418	1	12
β-strand	422-431	10	11
β-strand	439	1	11
β-strand	453	1	13
β-strand	456	1	14
β-strand	460-466	7	11
β-strand	476-478	3	13
β-strand	482-485	4	11
β-strand	508-514	7	11
α-helix	517-519	3
β-strand	529-534	6	13
α-helix	539-545	7
β-strand	549-553	5	13
β-strand	554	1	14
β-strand	572-580	9	15
α-helix	587-594	8
α-helix	606-609	4
β-strand	613-617	5	15
β-strand	620	1	15
β-strand	626	1	16
β-strand	634-641	8	15
β-strand	649-651	3	17
β-strand	652-653	2	18
β-strand	659	1	15
β-strand	664	1	15
β-strand	668-670	3	17
β-strand	674-681	8	15
β-strand	687	1	19
β-strand	689	1	16
β-strand	690-691	2	18
β-strand	705	1	16
β-strand	1695-1707	13	20
β-strand	1730-1738	9	20
α-helix	1754-1756	3
β-strand	1763-1765	3	21
β-strand	1770-1777	8	20
β-strand	1783	1	22
β-strand	1786	1	21
β-strand	1802	1	19
β-strand	1807	1	22
β-strand	1812-1818	7	20
α-helix	1819-1820	2
α-helix	1821-1823	3
β-strand	1832-1838	7	21
α-helix	1845-1848	4
β-strand	1852-1858	7	21
β-strand	1864	1	23
β-strand	1869	1	23
β-strand	1874-1884	11	24
α-helix	1889-1891	3
α-helix	1893-1895	3
α-helix	1913-1915	3
β-strand	1917-1921	5	24
β-strand	1924	1	24
β-strand	1933-1935	3	25
β-strand	1940-1946	7	24
β-strand	1955-1958	4	25
β-strand	1963-1967	5	24
β-strand	1969-1973	5	24
β-strand	1975-1977	3	25
β-strand	1983-1988	6	24
β-strand	1994-2000	7	25
α-helix	2003-2007	5
β-strand	2012-2017	6	25
β-strand	2023-2024	2	26
α-helix	2034-2036	3
β-strand	2037-2038	2	26
α-helix	2048-2050	3
β-strand	2052	1	26
β-strand	2062-2064	3	27
β-strand	2071-2086	16	26
β-strand	2090-2091	2	28
β-strand	2094-2095	2	28
β-strand	2097-2106	10	26
β-strand	2113-2114	2	26
α-helix	2124-2125	2
β-strand	2126-2127	2	26
β-strand	2136-2157	22	26
β-strand	2160-2162	3	27
β-strand	2164-2169	6	26
β-strand	2177	1	29
β-strand	2190-2192	3	30
α-helix	2205-2207	3
β-strand	2209	1	29
β-strand	2219	1	31
β-strand	2230-2233	4	30
β-strand	2238-2246	9	29
β-strand	2248-2250	3	32
β-strand	2253-2255	3	32
β-strand	2256-2265	10	30
β-strand	2272-2273	2	30
β-strand	2283	1	30
β-strand	2293	1	29
β-strand	2301	1	29
β-strand	2305-2314	10	30
β-strand	2316	1	30
β-strand	2319	1	31
β-strand	2320-2327	8	29

Chain B: 23 helices, 123 β-strands

Element	Residues	Length	Sheet
β-strand	2-6	5	33
β-strand	9-14	6	34
α-helix	19-25	7
β-strand	47-52	6	34
β-strand	55	1	33
α-helix	65-67	3
α-helix	68-70	3
β-strand	74-80	7	35
β-strand	84-89	6	33
β-strand	91	1	34
β-strand	97	1	36
β-strand	100-102	3	35
β-strand	105	1	33
α-helix	121-124	4
β-strand	129	1	36
β-strand	135-140	6	33
α-helix	143-145	3
β-strand	154-160	7	35
α-helix	165-171	7
β-strand	174-180	7	35
α-helix	184-186	3
β-strand	194-204	11	37
β-strand	231-235	5	37
β-strand	238	1	37
β-strand	247-249	3	38
β-strand	253-261	9	37
β-strand	268-269	2	39
β-strand	270-272	3	38
β-strand	275	1	38
β-strand	278	1	37
β-strand	288-289	2	39
β-strand	294-300	7	37
β-strand	305-311	7	38
β-strand	323-328	6	38
β-strand	381-394	14	40
β-strand	415	1	41
β-strand	418	1	41
β-strand	422-431	10	40
β-strand	439	1	40
β-strand	453-454	2	42
β-strand	460-468	9	40
β-strand	473	1	43
β-strand	476-477	2	42
β-strand	482-485	4	40
α-helix	498-500	3
β-strand	503	1	43
β-strand	508-514	7	40
α-helix	517-519	3
β-strand	528-534	7	42
α-helix	539-545	7
β-strand	548-554	7	42
β-strand	573-580	8	44
α-helix	587-594	8
α-helix	610-612	3
β-strand	613-617	5	44
β-strand	620	1	44
α-helix	622-624	3
β-strand	628-630	3	45
β-strand	634	1	46
β-strand	637-641	5	44
β-strand	649-651	3	47
β-strand	652-653	2	48
β-strand	659-660	2	49
β-strand	663-664	2	49
β-strand	668-670	3	47
β-strand	674-678	5	44
β-strand	679	1	49
β-strand	681	1	46
β-strand	686	1	50
β-strand	687	1	45
β-strand	690-691	2	48
α-helix	698-700	3
β-strand	703	1	48
β-strand	707-709	3	45
β-strand	1696-1702	7	51
β-strand	1704-1707	4	52
β-strand	1730-1733	4	52
β-strand	1736-1737	2	51
α-helix	1751-1756	6
β-strand	1763	1	53
β-strand	1766	1	54
β-strand	1770-1777	8	51
β-strand	1783	1	55
β-strand	1786	1	56
β-strand	1801	1	50
β-strand	1807	1	55
α-helix	1808	1
β-strand	1812-1818	7	51
α-helix	1821-1823	3
β-strand	1832	1	54
β-strand	1835	1	53
β-strand	1838	1	56
α-helix	1846-1849	4
β-strand	1852	1	56
β-strand	1855	1	53
β-strand	1858	1	54
β-strand	1874-1884	11	57
α-helix	1913-1916	4
β-strand	1917-1921	5	57
β-strand	1924	1	57
β-strand	1933-1935	3	58
β-strand	1940-1946	7	57
β-strand	1954-1958	5	58
β-strand	1963	1	59
β-strand	1964-1965	2	57
β-strand	1966-1967	2	60
β-strand	1969-1970	2	60
β-strand	1973	1	59
β-strand	1975-1978	4	58
β-strand	1984-1988	5	57
β-strand	1995-2000	6	58
α-helix	2003-2006	4
β-strand	2011-2017	7	58
β-strand	2037-2039	3	61
α-helix	2048-2050	3
β-strand	2052	1	61
β-strand	2062-2064	3	62
β-strand	2071-2088	18	61
β-strand	2091	1	63
β-strand	2094	1	63
β-strand	2097-2098	2	64
β-strand	2100-2106	7	61
β-strand	2113-2114	2	61
β-strand	2126-2127	2	61
β-strand	2133-2153	21	61
β-strand	2156-2157	2	64
β-strand	2160-2162	3	62
β-strand	2163-2169	7	61
β-strand	2176-2177	2	65
β-strand	2190-2192	3	66
α-helix	2205-2208	4
β-strand	2209	1	65
β-strand	2230-2233	4	66
β-strand	2242-2246	5	65
β-strand	2248-2249	2	67
β-strand	2254-2255	2	67
β-strand	2256	1	68
β-strand	2260-2265	6	66
β-strand	2272-2273	2	66
β-strand	2283	1	66
α-helix	2291-2292	2
β-strand	2293-2296	4	65
β-strand	2305-2310	6	66
β-strand	2314	1	68
β-strand	2316	1	68
β-strand	2320-2325	6	65

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Coagulation factor VIII chimera	A, B	protein	1467	Sus scrofa, Homo sapiens	P00451 (AlphaFold model), P12263 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>6MF0_1 Coagulation factor VIII chimera (chains A, B)
MQLELSTCVFLCLLPLGFSAIRRYYLGAVELSWDYRQSELLRELHVDTRFPATAPGALPL
GPSVLYKKTVFVEFTDQLFSVARPRPPWMGLLGPTIQAEVYDTVVVTLKNMASHPVSLHA
VGVSFWKSSEGAEYEDHTSQREKEDDKVLPGKSQTYVWQVLKENGPTASDPPCLTYSYLS
HVDLVKDLNSGLIGALLVCREGSLTRERTQNLHEFVLLFAVFDEGKSWHSARNDSWTRAM
DPAPARAQPAMHTVNGYVNRSLPGLIGCHKKSVYWHVIGMGTSPEVHSIFLEGHTFLVRH
HRQASLEISPLTFLTAQTFLMDLGQFLLFCHISSHHHGGMEAHVRVESCAEEPQLRRKAD
EEEDYDDNLYDSDMDVVRLDGDDVSPFIQIRSVAKKHPKTWVHYIAAEEEDWDYAPLVLA
PDDRSYKSQYLNNGPQRIGRKYKKVRFMAYTDETFKTREAIQHESGILGPLLYGEVGDTL
LIIFKNQASRPYNIYPHGITDVRPLYSRRLPKGVKHLKDFPILPGEIFKYKWTVTVEDGP
TKSDPRCLTRYYSSFVNMERDLASGLIGPLLICYKESVDQRGNQIMSDKRNVILFSVFDE
NRSWYLTENIQRFLPNPAGVQLEDPEFQASNIMHSINGYVFDSLQLSVCLHEVAYWYILS
IGAQTDFLSVFFSGYTFKHKMVYEDTLTLFPFSGETVFMSMENPGLWILGCHNSDFRNRG
MTALLKVSSCDKNTGDYYEDSYEDISAYLLSKNNAIEPRSFAQNSRPPSASAPKPPVLRR
HQRDISLPTFQPEEDKMDYDDIFSTETKGEDFDIYGEDENQDPRSFQKRTRHYFIAAVEQ
LWDYGMSESPRALRNRAQNGEVPRFKKVVFREFADGSFTQPSYRGELNKHLGLLGPYIRA
EVEDNIMVTFKNQASRPYSFYSSLISYPDDQEQGAEPRHNFVQPNETRTYFWKVQHHMAP
TEDEFDCKAWAYFSDVDLEKDVHSGLIGPLLICRANTLNAAHGRQVTVQEFALFFTIFDE
TKSWYFTENVERNCRAPCHLQMEDPTLKENYRFHAINGYVMDTLPGLVMAQNQRIRWYLL
SMGSNENIHSIHFSGHVFSVRKKEEYKMAVYNLYPGVFETVEMLPSKVGIWRIECLIGEH
LQAGMSTTFLVYSKKCQTPLGMASGHIRDFQITASGQYGQWAPKLARLHYSGSINAWSTK
EPFSWIKVDLLAPMIIHGIKTQGARQKFSSLYISQFIIMYSLDGKKWQTYRGNSTGTLMV
FFGNVDSSGIKHNIFNPPIIARYIRLHPTHYSIRSTLRMELMGCDLNSCSMPLGMESKAI
SDAQITASSYFTNMFATWSPSKARLHLQGRSNAWRPQVNNPKEWLQVDFQKTMKVTGVTT
QGVKSLLTSMYVKEFLISSSQDGHQWTLFFQNGKVKVFQGNQDSFTPVVNSLDPPLLTRY
LRIHPQSWVHQIALRMEVLGCEAQDLY

Ligands and cofactors

ID	Name	Formula	Copies
CU1	Copper (I) ion	Cu	2
ZN	Zinc ion	Zn	2
CA	Calcium ion	Ca	2

Primary citation

The 3.2 angstrom structure of a bioengineered variant of blood coagulation factor VIII indicates two conformations of the C2 domain. Smith, I.W., d'Aquino, A.E., Coyle, C.W. et al. J Thromb Haemost (2020) 18:57-69. DOI 10.1111/jth.14621 · PubMed

Other PDB entries of the same protein (UniProt P00451 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3HNY 1.07 Å, Factor VIII Trp2313-His2315 segment is involved in membrane binding as shown by crystal…
3HNB 1.15 Å, Factor VIII Trp2313-His2315 segment is involved in membrane binding as shown by crystal…
1D7P 1.5 Å, Crystal structure of the c2 domain of human factor viii at 1.5 a resolution at 1.5 A
9D5D 1.83 Å, Crystal Structure of Blood Coagulation Factor VIII C2 Domain Mutant L2251A/L2252A
1IQD 2.0 Å, Human Factor VIII C2 Domain complexed to human monoclonal BO2C11 Fab.
3HOB 2.07 Å, Factor VIII Trp2313-His2315 segment is involved in membrane binding as shown by crystal…
4PT6 2.1 Å, The discobody: an engineered discoidin domain from factor VIII that binds v 3 integrin…
4KI5 2.47 Å, Cystal structure of human factor VIII C2 domain in a ternary complex with murine…
4XZU 2.61 Å, Crystal Structure of the Human Factor VIII C2 Domain in Complex with Murine 3E6…
7KWO 2.9 Å, Rfviiifc-vwf-xten (BIVV001)
36JL 3.15 Å, Coagulation factor VIII, full-length, membrane-bound, on Ptd-choline : Ptd-serine 75:25…
9JBV 3.17 Å, Structure of Engineered Coagulation Factor VIII with Enhanced Secretion and Coagulation…

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