Cryo-EM structure of GGCX-MGP complex. Determined by electron microscopy at 3.33 Å resolution. Released 1 Apr 2026.
Explore 9WFC in 3D Show helices and sheets RCSB PDB PDBe
9WFC contains 44 α-helices and 22 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 33-38 | 6 | |
| α-helix | 42-44 | 3 | |
| α-helix | 48-55 | 8 | |
| β-strand | 58-59 | 2 | 1 |
| α-helix | 62-81 | 20 | |
| α-helix | 85-87 | 3 | |
| α-helix | 88-91 | 4 | |
| α-helix | 109-111 | 3 | |
| α-helix | 112-131 | 20 | |
| α-helix | 135-152 | 18 | |
| α-helix | 154-156 | 3 | |
| α-helix | 159-173 | 15 | |
| α-helix | 182-186 | 5 | |
| β-strand | 193 | 1 | 2 |
| β-strand | 195-196 | 2 | 1 |
| α-helix | 197-217 | 21 | |
| α-helix | 221-224 | 4 | |
| α-helix | 230-234 | 5 | |
| α-helix | 236-238 | 3 | |
| α-helix | 239-242 | 4 | |
| α-helix | 247-249 | 3 | |
| α-helix | 250-258 | 9 | |
| α-helix | 259-271 | 13 | |
| α-helix | 276-293 | 18 | |
| α-helix | 299-306 | 8 | |
| α-helix | 307-310 | 4 | |
| α-helix | 315-322 | 8 | |
| α-helix | 325-330 | 6 | |
| α-helix | 332-333 | 2 | |
| α-helix | 336-337 | 2 | |
| β-strand | 338 | 1 | 2 |
| α-helix | 339 | 1 | |
| α-helix | 358-376 | 19 | |
| α-helix | 377-382 | 6 | |
| α-helix | 385-387 | 3 | |
| β-strand | 405 | 1 | 3 |
| β-strand | 406-417 | 12 | 4 |
| β-strand | 423-426 | 4 | 4 |
| α-helix | 436-439 | 4 | |
| α-helix | 441-454 | 14 | |
| α-helix | 455-458 | 4 | |
| β-strand | 463-473 | 11 | 4 |
| α-helix | 476-477 | 2 | |
| β-strand | 478 | 1 | 5 |
| β-strand | 479-480 | 2 | 4 |
| β-strand | 482 | 1 | 6 |
| β-strand | 502 | 1 | 6 |
| α-helix | 503-505 | 3 | |
| α-helix | 507-509 | 3 | |
| α-helix | 510-522 | 13 | |
| β-strand | 527-534 | 8 | 5 |
| β-strand | 539-543 | 5 | 7 |
| β-strand | 549-557 | 9 | 5 |
| β-strand | 560-564 | 5 | 7 |
| β-strand | 569-573 | 5 | 7 |
| β-strand | 578-580 | 3 | 5 |
| β-strand | 586-591 | 6 | 7 |
| α-helix | 596 | 1 | |
| β-strand | 597-604 | 8 | 5 |
| α-helix | 606-617 | 12 | |
| α-helix | 657-674 | 18 | |
| α-helix | 677-708 | 32 | |
| α-helix | 713-724 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 20 | 1 | 3 |
| β-strand | 34 | 1 | 4 |
| α-helix | 37-40 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Vitamin K-dependent gamma-carboxylase | A | protein | 697 | Homo sapiens | P38435 (AlphaFold model) |
| Matrix Gla protein | B | protein | 28 | Homo sapiens | P08493 (AlphaFold model) |
>9WFC_1 Vitamin K-dependent gamma-carboxylase (chains A) SRIGKLLGFEWTDLSSWRRLVTLLNRPTDPASLAVFRFLFGFLMVLDIPQERGLSSLDRK YLDGLDVCRFPLLDALRPLPLDWMYLVYTIMFLGALGMMLGLCYRISCVLFLLPYWYVFL LDKTSWNNHSYLYGLLAFQLTFMDANHYWSVDGLLNAHRRNAHVPLWNYAVLRGQIFIVY FIAGVKKLDADWVEGYSMEYLSRHWLFSPFKLLLSEELTSLLVVHWGGLLLDLSAGFLLF FDVSRSIGLFFVSYFHCMNSQLFSIGMFSYVMLASSPLFCSPEWPRKLVSYCPRRLQQLL PLKAAPQPSVSCVYKRSRGKSGQKPGLRHQLGAAFTLLYLLEQLFLPYSHFLTQGYNNWT NGLYGYSWDMMVHSRSHQHVKITYRDGRTGELGYLNPGVFTQSRRWKDHADMLKQYATCL SRLLPKYNVTEPQIYFDIWVSINDRFQQRIFDPRVDIVQAAWSPFQRTSWVQPLLMDLSP WRAKLQEIKSSLDNHTEVVFIADFPGLHLENFVSEDLGNTSIQLLQGEVTVELVAEQKNQ TLREGEKMQLPAGEYHKVYTTSPSPSCYMYVYVNTTELALEQDLAYLQELKEKVENGSET GPLPPELQPLLEGEVKGGPEPTPLVQTFLRRQQRLQEIERRRNTPFHERFFRFLLRKLYV FRRSFLMTCISLRNLILGRPSLEQLAQEVTYANLRPF
>9WFC_2 Matrix Gla protein (chains B) LCYESHESMSYELNPFINRRNANTFISP
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 2 |
| POV | (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl… | C42 H82 N O8 P | 2 |
| MX7 | (2R)-3-(phosphonooxy)propane-1,2-diyl (9Z,9'Z)bis-octadec-9-enoate | C39 H73 O8 P | 1 |
| CLR | Cholesterol | C27 H46 O | 1 |
| A1AT1 | (1aR,7aS)-1a-methyl-7a-[(2E,6E,10E)-3,7,11,15-tetramethylhexadeca-2,6,10,14-tet… | C31 H40 O3 | 1 |
Cryo-EM structure of GGcX-MGP complex. Qian, H.W., Zhang, W.J. To be published.
Other PDB entries of the same protein (UniProt P38435 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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