9BUX: GGCX-BGP-menaquinone-4 epoxide complex

Structure of GGCX-BGP-menaquinone-4 epoxide complex. Determined by electron microscopy at 3.06 Å resolution. Released 29 Jan 2025.

Method
Electron microscopy
Resolution
3.06 Å
Organism
Homo sapiens
Chains
2
Atoms
5,861
Mol. weight
102.93 kDa
Ligands
NAG, CLR, POV, A1AT1
Released
29 Jan 2025

Explore 9BUX in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9BUX contains 38 α-helices and 20 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: 37 helices, 19 β-strands

ElementResiduesLengthSheet
α-helix35-384
α-helix42-454
α-helix49-557
β-strand5911
α-helix62-7615
α-helix78-814
α-helix108-1114
α-helix112-13120
α-helix135-15117
α-helix154-1563
α-helix159-17315
α-helix183-1864
β-strand19312
β-strand19511
α-helix198-21720
α-helix221-2244
α-helix232-2343
α-helix236-2383
α-helix241-2433
α-helix247-2493
α-helix250-2578
α-helix260-2645
α-helix276-29318
α-helix299-3057
α-helix307-3093
α-helix315-3206
α-helix336-3372
β-strand33812
α-helix3391
α-helix358-37316
α-helix377-3793
β-strand406-416113
β-strand423-42643
α-helix441-45414
α-helix455-4584
β-strand466-47383
β-strand47814
β-strand479-48023
β-strand48215
β-strand50215
α-helix503-5053
α-helix507-5093
α-helix513-5219
β-strand527-53484
β-strand539-54356
β-strand551-55774
β-strand560-56456
β-strand569-57246
β-strand578-58144
β-strand586-59166
α-helix5961
β-strand597-60484
α-helix606-62217
α-helix655-67319
α-helix677-70731
α-helix713-72311
Chain B: 1 helix, 1 β-strand
ElementResiduesLengthSheet
β-strand36-3723
α-helix89-957

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Vitamin K-dependent gamma-carboxylaseAprotein766Homo sapiensP38435 (AlphaFold model)
OsteocalcinBprotein106Homo sapiensP02818 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>9BUX_1 Vitamin K-dependent gamma-carboxylase (chains A)
MAVSAGSARTSPSSDKVQKDKAELISGPRQDSRIGKLLGFEWTDLSSWRRLVTLLNRPTD
PASLAVFRFLFGFLMVLDIPQERGLSSLDRKYLDGLDVCRFPLLDALRPLPLDWMYLVYT
IMFLGALGMMLGLCYRISCVLFLLPYWYVFLLDKTSWNNHSYLYGLLAFQLTFMDANHYW
SVDGLLNAHRRNAHVPLWNYAVLRGQIFIVYFIAGVKKLDADWVEGYSMEYLSRHWLFSP
FKLLLSEELTSLLVVHWGGLLLDLSAGFLLFFDVSRSIGLFFVSYFHCMNSQLFSIGMFS
YVMLASSPLFCSPEWPRKLVSYCPRRLQQLLPLKAAPQPSVSCVYKRSRGKSGQKPGLRH
QLGAAFTLLYLLEQLFLPYSHFLTQGYNNWTNGLYGYSWDMMVHSRSHQHVKITYRDGRT
GELGYLNPGVFTQSRRWKDHADMLKQYATCLSRLLPKYNVTEPQIYFDIWVSINDRFQQR
IFDPRVDIVQAAWSPFQRTSWVQPLLMDLSPWRAKLQEIKSSLDNHTEVVFIADFPGLHL
ENFVSEDLGNTSIQLLQGEVTVELVAEQKNQTLREGEKMQLPAGEYHKVYTTSPSPSCYM
YVYVNTTELALEQDLAYLQELKEKVENGSETGPLPPELQPLLEGEVKGGPEPTPLVQTFL
RRQQRLQEIERRRNTPFHERFFRFLLRKLYVFRRSFLMTCISLRNLILGRPSLEQLAQEV
TYANLRPFEAVGELNPSNTDSSHSNPPESNPDPVHSEFDYKDDDDK
Sequence of entity 2 (B), FASTA
>9BUX_2 Osteocalcin (chains B)
MRALTLLALLALAALCIAGQAGAKPSGAESSKGAAFVSKQEGSEVVKRPRRYLYQWLGAP
VPYPDPLEPRREVCELNPDCDELADHIGFQEAYRRFYGPVHHHHHH

Ligands and cofactors

IDNameFormulaCopies
NAG2-acetamido-2-deoxy-beta-D-glucopyranoseC8 H15 N O62
CLRCholesterolC27 H46 O1
POV(2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl…C42 H82 N O8 P1
A1AT1(1aR,7aS)-1a-methyl-7a-[(2E,6E,10E)-3,7,11,15-tetramethylhexadeca-2,6,10,14-tet…C31 H40 O31

Primary citation

Structure and mechanism of vitamin-K-dependent gamma-glutamyl carboxylase. Wang, R., Chen, B., Elghobashi-Meinhardt, N. et al. Nature (2025) 639:808-815. DOI 10.1038/s41586-024-08484-9 · PubMed

Other PDB entries of the same protein (UniProt P38435 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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