36JL: Coagulation factor VIII

Coagulation factor VIII, full-length, membrane-bound, on Ptd-choline : Ptd-serine 75:25 vesicles. Determined by electron microscopy at 3.15 Å resolution. Released 16 Sept 2026.

Method
Electron microscopy
Resolution
3.15 Å
Organism
Homo sapiens
Chains
1
Atoms
9,744
Mol. weight
266.66 kDa
Ligands
CPS, SEP, CU1, CA
Released
16 Sept 2026

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

Secondary structure: helices and β-sheets

36JL contains 27 α-helices and 105 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: 27 helices, 105 β-strands

ElementResiduesLengthSheet
β-strand2-14131
β-strand46-5381
β-strand5412
β-strand6212
α-helix63-664
α-helix67-693
α-helix721
β-strand73-7863
β-strand82-9091
β-strand9614
β-strand9913
β-strand10411
α-helix107-1093
α-helix121-1266
β-strand12814
β-strand133-14081
α-helix142-1443
β-strand153-15973
α-helix164-1707
β-strand173-17973
β-strand195-20395
α-helix204-2063
β-strand230-23455
β-strand23715
α-helix239-2413
β-strand245-24846
β-strand253-26085
β-strand267-27156
β-strand276-27835
β-strand281-28335
β-strand286-28836
β-strand293-29865
β-strand304-31076
α-helix313-3153
β-strand322-32766
β-strand38117
β-strand387-38828
β-strand390-39459
α-helix407-4115
β-strand422-42659
β-strand42918
β-strand453-456410
β-strand46017
β-strand464-46748
β-strand473111
β-strand476-478310
β-strand482-48547
α-helix501-5022
β-strand503111
α-helix5041
β-strand508-51038
β-strand511-51447
β-strand528-534710
α-helix539-5446
β-strand549-554610
β-strand572-580912
α-helix587-5915
α-helix606-6094
β-strand613-617512
β-strand620112
β-strand622-629813
β-strand633-641912
β-strand649-652414
β-strand658-660312
β-strand663-665312
β-strand667-670414
β-strand675-682812
β-strand686-688313
β-strand691-692214
α-helix695-6984
β-strand703-708613
β-strand1695-17071315
β-strand1730-1738915
β-strand1746115
α-helix1747-17493
α-helix1754-17563
β-strand1763-1766416
β-strand1770-1776715
β-strand1783117
β-strand1786-1787216
β-strand1807117
β-strand1812-1818715
α-helix1821-18233
β-strand1832-1838716
α-helix1845-18495
β-strand1853-1858616
β-strand1864118
β-strand1869118
β-strand1874-18841119
α-helix1885-18873
α-helix1891-18988
β-strand1917-1921519
β-strand1924119
β-strand1933-1935320
β-strand1940-1946719
β-strand1954-1958520
β-strand1963-1966419
β-strand1970-1973419
β-strand1975-1978420
β-strand1980119
β-strand1984-1988519
β-strand1994-2000720
α-helix2003-20086
β-strand2011-2017720
β-strand2023-2024221
α-helix2034-20363
β-strand2037-2039321
β-strand2043122
β-strand2046122
α-helix2048-20503
β-strand2062-2064323
β-strand2071-20871721
β-strand2097-21061021
β-strand2113-2114221
β-strand2126-2127221
β-strand2136-21572221
β-strand2159121
β-strand2160-2162323
β-strand2163-2169721
β-strand2177124
α-helix2187-21893
β-strand2192124
β-strand2197125
β-strand2202125
β-strand2230-22451624
β-strand2248-2250326
β-strand2253-2255326
β-strand2260-2265624
β-strand2272-2273224
β-strand2283124
β-strand2293-23101824
β-strand2322-2327624

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Coagulation factor VIIIAprotein2332Homo sapiensP00451 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>36JL_1 Coagulation factor VIII (chains A)
ATRRYYLGAVELSWDYMQSDLGELPVDARFPPRVPKSFPFNTSVVYKKTLFVEFTDHLFN
IAKPRPPWMGLLGPTIQAEVYDTVVITLKNMASHPVSLHAVGVSYWKASEGAEYDDQTSQ
REKEDDKVFPGGSHTYVWQVLKENGPMASDPLCLTYSYLSHVDLVKDLNSGLIGALLVCR
EGSLAKEKTQTLHKFILLFAVFDEGKSWHSETKNSLMQDRDAASARAWPKMHTVNGYVNR
SLPGLIGCHRKSVYWHVIGMGTTPEVHSIFLEGHTFLVRNHRQASLEISPITFLTAQTLL
MDLGQFLLFCHISSHQHDGMEAYVKVDSCPEEPQLRMKNNEEAEDYDDDLTDSEMDVVRF
DDDNSPSFIQIRSVAKKHPKTWVHYIAAEEEDWDYAPLVLAPDDRSYKSQYLNNGPQRIG
RKYKKVRFMAYTDETFKTREAIQHESGILGPLLYGEVGDTLLIIFKNQASRPYNIYPHGI
TDVRPLYSRRLPKGVKHLKDFPILPGEIFKYKWTVTVEDGPTKSDPRCLTRYYSSFVNME
RDLASGLIGPLLICYKESVDQRGNQIMSDKRNVILFSVFDENRSWYLTENIQRFLPNPAG
VQLEDPEFQASNIMHSINGYVFDSLQLSVCLHEVAYWYILSIGAQTDFLSVFFSGYTFKH
KMVYEDTLTLFPFSGETVFMSMENPGLWILGCHNSDFRNRGMTALLKVSSCDKNTGDYYE
DSYEDISAYLLSKNNAIEPRSFSQNSRHPSTRQKQFNATTIPENDIEKTDPWFAHRTPMP
KIQNVSSSDLLMLLRQSPTPHGLSLSDLQEAKYETFSDDPSPGAIDSNNSLSEMTHFRPQ
LHHSGDMVFTPESGLQLRLNEKLGTTAATELKKLDFKVSSTSNNLISTIPSDNLAAGTDN
TSSLGPPSMPVHYDSQLDTTLFGKKSSPLTESGGPLSLSEENNDSKLLESGLMNSQESSW
GKNVSSTESGRLFKGKRAHGPALLTKDNALFKVSISLLKTNKTSNNSATNRKTHIDGPSL
LIENSPSVWQNILESDTEFKKVTPLIHDRMLMDKNATALRLNHMSNKTTSSKNMEMVQQK
KEGPIPPDAQNPDMSFFKMLFLPESARWIQRTHGKNSLNSGQGPSPKQLVSLGPEKSVEG
QNFLSEKNKVVVGKGEFTKDVGLKEMVFPSSRNLFLTNLDNLHENNTHNQEKKIQEEIEK
KETLIQENVVLPQIHTVTGTKNFMKNLFLLSTRQNVEGSYDGAYAPVLQDFRSLNDSTNR
TKKHTAHFSKKGEEENLEGLGNQTKQIVEKYACTTRISPNTSQQNFVTQRSKRALKQFRL
PLEETELEKRIIVDDTSTQWSKNMKHLTPSTLTQIDYNEKEKGAITQSPLSDCLTRSHSI
PQANRSPLPIAKVSSFPSIRPIYLTRVLFQDNSSHLPAASYRKKDSGVQESSHFLQGAKK
NNLSLAILTLEMTGDQREVGSLGTSATNSVTYKKVENTVLPKPDLPKTSGKVELLPKVHI
YQKDLFPTETSNGSPGHLDLVEGSLLQGTEGAIKWNEANRPGKVPFLRVATESSAKTPSK
LLDPLAWDNHYGTQIPKEEWKSQEKSPEKTAFKKKDTILSLNACESNHAIAAINEGQNKP
EIEVTWAKQGRTERLCSQNPPVLKRHQREITRTTLQSDQEEIDYDDTISVEMKKEDFDIY
DEDENQSPRSFQKKTRHYFIAAVERLWDYGMSSSPHVLRNRAQSGSVPQFKKVVFQEFTD
GSFTQPLYRGELNEHLGLLGPYIRAEVEDNIMVTFRNQASRPYSFYSSLISYEEDQRQGA
EPRKNFVKPNETKTYFWKVQHHMAPTKDEFDCKAWAYFSDVDLEKDVHSGLIGPLLVCHT
NTLNPAHGRQVTVQEFALFFTIFDETKSWYFTENMERNCRAPCNIQMEDPTFKENYRFHA
INGYIMDTLPGLVMAQDQRIRWYLLSMGSNENIHSIHFSGHVFTVRKKEEYKMALYNLYP
GVFETVEMLPSKAGIWRVECLIGEHLHAGMSTLFLVYSNKCQTPLGMASGHIRDFQITAS
GQYGQWAPKLARLHYSGSINAWSTKEPFSWIKVDLLAPMIIHGIKTQGARQKFSSLYISQ
FIIMYSLDGKKWQTYRGNSTGTLMVFFGNVDSSGIKHNIFNPPIIARYIRLHPTHYSIRS
TLRMELMGCDLNSCSMPLGMESKAISDAQITASSYFTNMFATWSPSKARLHLQGRSNAWR
PQVNNPKEWLQVDFQKTMKVTGVTTQGVKSLLTSMYVKEFLISSSQDGHQWTLFFQNGKV
KVFQGNQDSFTPVVNSLDPPLLTRYLRIHPQSWVHQIALRMEVLGCEAQDLY

Ligands and cofactors

IDNameFormulaCopies
CPS3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonateC32 H58 N2 O7 S1
SEPPhosphoserineC3 H8 N O6 P2
CU1Copper (I) ionCu2
CACalcium ionCa1
NAG2-acetamido-2-deoxy-beta-D-glucopyranoseC8 H15 N O62

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 P00451 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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